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- Bad Boy Wake / Rocky Primavera Rocky Primavera Never received product and every excuse on why its not here then nothing. He has all my Money Port Alberni, British Columbia
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- BAD BOY WAKE ROCKY JOHN PRIMAVERA THIEF, Does not send items ordered, Will have lots of excuses of why the shipment is late. After 45 days will cut off contact. PORT ALBERNI, British Columbia
- Paws & Claws Corey Samuel Scam Artist Kelowna Nationwide
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- COLLIN J TOWERS GLAMOR IN ALANTA GEORGIA RIPPS OFF MODELS,AND REPORTS THAT HE DOES RIP WOMEN OFF i KNOW FOR A FACT i USE TO WORK FOR HIM. ALANTA, Georgia
- Bernie lynch Bernard Lynch We are building a case & are looking for additional info. They Sold us heaters that were supposed to be CSA & Ontario Hydro approved for the rental market. They were not CSA & don't work. Niagara Falls, Ontario Canada
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- Report: #913631
bad boy wake towers
bad boy wake towers6106 Cottam Road Port Alberni, British Columbia United States of America
bad boy wake towers costal cleaning asked for money up front with a promised better deal and never sends product, have been waiting since feb,2012 never returns calls or emails once he has your cash Port Alberni, British Columbia
*Author of original report: medic33
*General Comment: Please Help
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This report was posted on Ripoff Report on 07/17/2012 09:25 PM and is a permanent record located here: http://www.ripoffreport.com/reports/bad-boy-wake-towers/port-alberni-british-columbia-v9y-8r9/bad-boy-wake-towers-costal-cleaning-asked-for-money-up-front-with-a-promised-better-deal-a-913631. The posting time indicated is Arizona local time. Arizona does not observe daylight savings so the post time may be Mountain or Pacific depending on the time of year.
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#1 Author of original report
AUTHOR: djsav - ()
SUBMITTED: Sunday, May 26, 2013POSTED: Sunday, May 26, 2013
i know everything there is to know about this guy and have gotten ahold of him which he started he would send me the product within the next week. if i dont hear from him i do have a couple of assotiates that know about him and his family on the island. basically if you would like your product or cash back let me know and i will have them colect for you. not sure how you can contact me but if you can get me your contact info i would be happy to help
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AUTHOR: medic33 - (Canada)
SUBMITTED: Thursday, January 03, 2013POSTED: Thursday, January 03, 2013
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When you meet Madhuri Bhatia, make sure you have lots of time at hand for she loves to chat and share notes. An animated conversation with her is sure to boost your adrenaline, more than any bungey jumping experiment. Trust me when I say this, you will return an enriched soul after meeting her.
Actor, jazz singer, voiceover artist, yoga practitioner, danseuse, choreographer and most importantly, an unassuming and a very interesting personality, Madhuri Bhatia is all this and much more. Her artistically-designed and meticulously-maintained abode in Andheri, Mumbai reflects her personality.
Single but always ready to mingle, this 64-year-old feisty lady blessed with a distinct voice believes talent is only a potential and is of use only when converted in to a skill. One can learn only this much on-the-job. "While desire is simply the foundation, only a marriage of rigorous training and talent can result in its success in any field. One has to keep upgrading to avoid becoming stagnant," asserts Bhatia.
After completing Bachelor of Performing Arts (B.P.A) from Shriram Bharatiya Kala Kendra in New Delhi, Bhatia also pursued a diploma in Hath Yoga and Pranayam and classical Indian dance technique Mayurbhanj Chhaau from the same institution. She studied western music with Paramvir and Zohra Shaw.
She does not particularly like the term 'celebrity' and says one should compete with oneself and never pull others down or ride on anyone's shoulders, a common trend in the showbiz industry. "I feel happier when people appreciate my work, not just when I am asked for autographs or photo-ops. She stated she was glad to be in an era when so much of experimental work in the arts was taking place.
Her list of films in India and Canada includes Pardes, Kites, My Bollywood Bride, Masala, Dreams Of The Night Cleaners and The Kalani of Shiva. Her TV shows include Kahin To Hogaa, Kuch Is Tarah, Harry's Case, Relic Hunter and many more.
She has conducted and participated in several workshops on improvisation, scene and character study, movement and voice. As a voiceover artiste, she has worked in several voicing projects on a regular basis with Disney, E-learning and assorted narrations in Hindi and English.
Ruing that physical appearance has become the most important pre-requisite of acting, Bhatia said, "Botox or the lack of it is not going to make you a better actor. Being obsessed with one's physicality is counter-productive. One has to come to terms with what one has and work with it".
It is arrogance to think, 'I have made it by myself'. We are where we are because of the support we receive from our relationships and the environment, pointed Bhatia.
She has been awarded the New York Bronze (Acting) in Toronto, Canada and A .V.A. Bronze for voicing in Mumbai. She believes that each of us is special in our own ways. "Some people are good at their work and are recognized. Unfortunately, some people of caliber are never given the opportunity.
Instead of attempting to be different, one should just concentrate on doing an assignment well, she added. Bhatia believes, "The satisfaction that lies in the process of creating is the utimate essence of beauty".
A globe trotter, she has a vast, varied and an amazing collection of books, trinkets and music albums.
As a child, she was once slapped by her Pakistan-born father for asking, "What is my caste?" She grew up listening to her father reading excerpts from various spiritual books and her mother listening to classical Indian and western musical notes. "We, humans, should learn to take ourselves lightly and laugh at ourselves. Religion is best confined to our homes. In fact, the only religion of value is one's value system," she stated.
Pics by Farooq Sayed


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Road to longevity and best of health
For those people who have already embarked on the road to those more "mature" years of their lives, each aspect can be said to influence it to a certain extent. One of the factors that seem to be the most prominent and influential is nutrition. A proper one can and certainly does promote not only a much better and satisfactory health, but it also makes it possible for a person to recharge those energy sources and restore and increase the overall energy, which is essential as a part of the rejuvenation process. In addition, when all pieces in places, one is most definitely going to feel much better than he/she did prior to incorporating proper lifestyle habits.
Astonishing eye-openers
What have scientists and experts in the field of diet and nutrition revealed by way of conducting carefully designed research studies, can be said to be somewhat shocking and concerning. Namely, the greatest majority of people today have been found to consume all too small variety of food, which means that they introduce little or no diversity when it comes to their daily meals. In addition, and having an average household and family in mind, the fact which is shocking is that just six to seven different varieties of meals are at one's choosing day in and day out.
More importantly, what the overall statistics have shown is that a nutrition that has been chosen properly and with great care makes those visits to the doctor astonishingly less frequent and in many cases quite unnecessary, particularly in cases of seniors. However, in case a person is experiencing certain problems and complications which are medical in nature, he/she should not hesitate and abstain from paying their physician a visit for the purpose of acquiring useful advice, as well as recommendations on how to make their health much better.
Importance of senior nutrition
Having nutrition and this specific target group in mind, it cannot be emphasized enough how vital the most proper nutrition, in combination with other factors, is in terms of optimal health. Aside from nutrition, regarded as extremely important is getting up from the bed in the morning hours, feeling quite rested and vigorous. Thus, proper rest is also vital.
In order to make this much easier, a senior should follow advice given by the physician and nutritionist as best as possible, complemented with off-medical research on what a proper nutrition in the "autumn of one's life" should look like and what it should be based on. This is the surest way to great health and longevity.
- Photo courtesy of U.S. Department of Agriculture by Flickr: www.flickr.com/photos/41284017@N08/4606298909


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Peptide generation by the UPS (ubiquitin–proteasome system) is rate-limiting in MHC class I-restricted antigen presentation in response to virus-induced IFNs (interferons). In this process, the role of IFN-induced rapid remodelling of the UPS is less defined. IFN-mediated de novo formation of different proteasome compositions as i20S (immunoproteasomes) or m20S (mixed-type proteasomes) essentially supports the rapid adjustment of the mammalian immune system to pathogens. This adjustment is of particular importance for the immune response to rapidly replicating viruses. In agreement, i20S formation has been shown to be an accelerated and transient response. Moreover, i20S and/or PA28 (proteasome activator 28) are essentially required for the generation of certain viral epitopes. In the present paper, we discuss how IFNs consecutively regulate the UPS at different levels, thereby improving the immune responsiveness of target cells.
- antigen presentation
- immune response
- interferon (IFN)
- proteasome
- ubiquitin–proteasome system
The UPS (ubiquitin–proteasome system)
Conjugation of proteins with ubiquitin modifiers or UBLs (ubiquitin-like proteins) represents a post-translational modification signal involved in the regulation of a variety of cellular responses [1]. Depending on the kind of ubiquitination, different pathways can be utilized: polyubiquitin chains at substrates serve as a signal for their selective degradation by the proteasome. On the other hand, mono-ubiquitination of protein targets is involved in signalling or endocytosis [2]. Thus the UPS controls intracellular protein homoeostasis and quality and the availability of regulator proteins and it generates antigenic peptides for the recognition of viral or tumorigenic transformed target cells by CTL (cytotoxic T-lymphocyte) [1,3–5].
Protein substrates become tagged with ubiquitin or UBLs in an ATP-dependent manner by a three-step process involving the sequential action of the ubiquitin-activating enzyme E1, several cognate E2 ubiquitin-conjugating enzymes and a series of substrate-specific E3 ubiquitin ligases that physically interact with the substrate to transfer ubiquitin moieties. Multiple DUBs (deubiquitinating enzymes) can counteract this process and remove the ubiquitin or UBL tag [1,3,4]. In this context, it is important to note that more than 1000 components related to the mammalian UPS have so far been identified to be involved in ubiquitin conjugation, deconjugation, substrate recognition and degradation. In addition to more than 40 different subunits of the proteasome, the human genome encodes 15 E1-isoforms that can activate ubiquitin or ten other UBLs. Moreover, 77 family members of the E2 enzymes and more than 600 monomeric E3 ligases or components of multimeric E3 ligases have been recognized [4]. Furthermore, there exist various proteins containing ubiquitin domains, proteins with ubiquitin interaction domains that often serve as adaptors and more than 90 DUBs [4].
Polyubiquitinated substrates are degraded by the 26S proteasome consisting of the catalytic 20S core complex capped by one or two 19S regulatory particles [5]. The 20S particles comprise four staggered rings, each containing seven non-identical subunits. The outer rings contain the α-subunits (α1–α7), which form the 'gates' through which substrates enter and products are released. In addition to the 19S regulatory complex, the PA28 (proteasome activator 28) can interact with the α-ring of the 20S complex, which opens the gates and may support the generation of antigenic peptides [6]. Each of the two inner rings contain the β-subunits (β1–β7), three of which (β1, β2 and β5) harbour the six active sites [7,8]. In addition, specific catalytically active proteasome subunits referred to as immunosubunits [9] are incorporated into alternative proteasome compositions and improve antigen processing [10–12].
Thus there exist at least two types of proteasomes, namely s20S (standard proteasomes) that are constitutively expressed in all cells and i20S (immunoproteasomes) that are formed on exposure of cells to IFNs (interferons). Additionally, the so-called intermediate proteasomes or m20S (mixed-type proteasomes) were found in different tissues that contain constitutive as well as immunosubunits and have been shown to be enzymatically active [13,14].
Regulation of proteasomal activities by incorporation of subunits
Proteasome subtypes are exclusively formed de novo following a sophisticated and not yet fully understood biogenesis programme involving the biosynthesis of all subunits, their assembly and maturation processes [15]. Thus proteasomal activities are controlled at the level of subunit expression, subunit incorporation and the maturation dynamics of the active sites.
After biosynthesis of all subunits, current assembly models for eukaryotic 20S proteasomes assume that the initial assembly step is the formation of a heptameric α-ring serving as a matrix for the subsequent incorporation of β-subunits [15]. Active-site β-subunits are incorporated as proproteins that essentially mature by an autocatalytic, two-step procedure within the precursor complexes. The removal of the β-subunit-propeptides liberates the active-site threonine residues of the now active 20S core proteasome [15–18]. Co-ordinated assembly of proteasomes requires helper factor as the mammalian POMP (proteasome maturation protein), which facilitates the recruitment and co-ordinate processing of the β-subunits, thereby becoming the first substrate of the activated 20S proteasome. Thus degradation of POMP signals the successful completion of the biogenesis programme [19]. Incorporation and maturation dynamics of active-site β-subunits are strictly determined by their propeptides [19–22]. This phenomenon becomes especially apparent in human cancer cells expressing the non-functional immunosubunit variant LMP7E1 (low-molecular-mass protein 7E1) bearing an alternative propeptide. The molecular explanation for this phenomenon is the incapacity of LMP7E1 to interact with POMP, which results in i20S deficiency [23].
Major steps in the formation of c20S and i20S take place at the ER (endoplasmic reticulum) surface by a POMP-mediated mechanism. Thereby POMP interacts with ER membranes, binds α1–7 rings, recruits β-subunits and mediates the association of POMP-containing precursor complexes with the ER. This ER-associated proteasome formation can ensure a sufficient supply of newly formed proteasomes to fulfil its roles in ER-associated protein degradation and generation of antigenic peptides, which are transported into the ER [24] (Figure 1).
It is well known that type II IFNs (IFN-γ) induce the synthesis of the so-called immunosubunits, β1i/LMP2, β2i/MECL1 (multicatalytic endopeptidase complex-like 1) and β5i/LMP7, which are co-operatively incorporated into nascent proteasomes, thereby replacing their constitutive homologues β1, β2 and β5 [16,18,25]. Immunosubunits together with other components of the APM (antigen presentation machinery) can also be induced rapidly by type I IFNs (IFN-α and -β) prior to IFN-γ action [26–28]. IFN-α and -β are a family of secreted cytokines induced as a very early response to viral infection of eukaryotic cells. Whereas almost all cell types secrete type I IFNs at low levels, haemopoietic cells are the major source of IFN-α and fibroblasts are major producers of IFN-β. Type I IFNs exhibit both autocrine and paracrine effects by stimulation of neighbouring cells and recruitment of NK cells (natural killer cells) to produce IFN-γ during the first day after infection [29,30]. As a result of the fast IFN secretion, immunosubunits are rapidly induced and incorporated into nascent proteasomes.
Interestingly, IFN-γ also enhanced POMP mRNA levels, suggesting that POMP may play an important role in i20S biogenesis [19]. Investigation of the kinetics, the molecular role of POMP, β5i/LMP7 and proteasome turnover in this proteasomal immune adaptation revealed answers to the question of how cells regulate proteasome levels in response to IFNs. Taking POMP turnover as a signal for completion of biogenesis, i20S are formed 4-fold faster than s20S. This high turnover of POMP is strictly dependent on the induction of a functional β5i/LMP7. Both components, POMP and β5i/LMP7, are essential for the rapid up-regulation of i20S formation by physical interaction. Silencing of POMP by RNA interference resulted in accumulation of ubiquitinated proteasomal substrates, reduced MHC I surface expression and ultimately cell death [22]. In combination with the observed drastically reduced half-life of i20S compared with s20S, our experiments explain that proteasomal immune adaptation is a highly dynamic and transient response [22].
In tissues and organs, the formation of different proteasome species is consistently more complex, since IFNs also induce the formation of m20S complexes. Even in lymphatic cells the i20S content does not exceed a critical limit of 60% of the total proteasome content [31,32]. Thus a varying mixture of different proteasome compositions seems to constitute the cellular proteasome pool depending on environmental requirements. In addition to type I IFNs, i20S formation in human target cells can also be induced by infection with HCV (hepatitis C virus), which cannot be further increased by IFNγ release in vivo [27,28]. Soon after an immunological challenge, when 20S complexes are formed de novo, the cellular proteasome population is remodelled in its subtypes and also in its functional properties. Thus this mechanism has a direct impact on the resulting immune response [31,32]. In detail, i20S serves a dual role in infected and non-infected cells. Secretion of IFNs in response to infection results in a fast i20S formation, which maintains protein homoeostasis and generates pathogen-derived epitopes in parallel. Thereby such cells are labelled as target cells for destruction by specific CTLs. In contrast, in non-infected cells, i20S are especially responsible for the preservation of intracellular protein balance. Thus proteasomal immune adaptation is rapid enough to contribute to an efficient immune response and permits the fast return to the constitutive situation once i20S function is not required any more. This mechanism is especially important in infected tissues to reduce massive cellular damage of surrounding tissue (Figure 2).
In conclusion, the formation pathway of different proteasome types constitutes an important cellular control mechanism for the quality and quantity of proteasome-mediated protein degradation and/or antigen presentation in both the regulatory as well as the scavenger sense.
The role of the UPS in response to IFNs and infections
MHC class I-restricted antigen presentation is an essential step in the priming of CD8+ T-lymphocytes by professional antigen-presenting cells as well as for the elimination of infected target cells by CTLs during immune responses to infection. The kinetics of in vivo priming of CD8+ T-cells by antigen presentation turned out to be surprisingly rapid and transient, since pathogen-specific T-lymphocytes were programmed during the first 24 h and the priming capacity lasted only 72 h in a Listeria infection model [33].
Peptide generation by the UPS is rate-limiting in MHC class I-restricted antigen presentation [34]. Thus the UPS is an essential component of an efficient immune system. In order to conserve the balance of protein synthesis and turnover, freshly translated polypeptides and short-lived proteins represent a main source of proteasomal substrates [35,36]. An increasing number of reports indicate that defined antigenic peptides derive from such freshly translated polypeptides. These peptides are assumed to be generated by a subset of ribosomes, the so-called 'immunoribosomes' in response to infections, and are further degraded by proteasomes after ubiquitination [37]. This is especially important during viral infections as many viruses can replicate rapidly and high amounts of antigenic peptides have to be generated from viral proteins in very short times, which results in a rapid CTL response [38]. Viral infections can induce also an increased generation of defective ribosomal products by manipulation of the host cell translational machinery, which additionally contributes to an enhanced MHC class I loading. In this context, modifications of the translation efficiency have been observed in cells infected with Semliki Forest virus and in target cells expressing a truncated EBV (Epstein–Barr virus)-encoded nuclear antigen 1 protein [39,40]. A regulated activity of translation also seems to be crucial during dendritic cell maturation and is in line with MHC class I-restricted antigen presentation derived from newly synthesized proteins [41].
The connection of the UPS to antigen presentation
Efficient elimination of virus-infected target cells by CTLs can only occur by a rapid MHC class I antigen presentation of viral epitopes on the cell surface. To cope with rapidly replicating viruses without delay, the immune system of a challenged organism requires the timely formation and availability of i20S. All known data indicate that IFN-mediated induction of i20S can improve MHC class I antigen presentation by more efficient production of certain viral peptides [5,12,15]. The most drastic effects have been described for the generation of the epitope of the hepatitis B virus core antigen [42] and the influenza A matrix protein M1 ([43] and S. Urban, E. Krüger and U. Seifert, unpublished work), which are completely dependent on i20S. An important role for i20S could also be observed when we analysed the generation of an epitope (HCV-NS31073–1081) derived from the HCV-NS3 protein. Comparison of the NS3987–1133 sequence derived from an infectious source with sequences that we isolated from sera of persistently infected patients revealed a high mutation rate at NS31082. This position is located directly adjacent to the epitope's C-terminus and affects proteasomal processing negatively. i20S appeared to digest the wild-type polypeptide more rapidly than the c20S, resulting in a more efficient epitope generation [44]. The importance of the rapid i20S formation was also analysed by generation of antigenic peptides derived from Listeria monocytogenes in mice lacking the immunosubunits β5i/LMP7 and β2i/MECL1. Besides the inability of i20S-deficient mice to generate CTLs against the epitope E1B192–200, it turned out to be important and rate-limiting that antigen processing occurs early during infection [45]. Moreover, formation of i20S is especially important for the determination of MHC class I epitope hierarchy [46].
Direct evidence that the composition of 20S particles is more complex in living cells or organisms and has an impact on epitope generation derives from experiments with cells and mice expressing different m20S compositions. It has been observed that the generation of the melanoma epitope (MART26–35, where MART is melanoma antigen recognized by T-cells) was impaired by complete i20S, whereas epitope generation was sufficient in β1i/LMP2-knockout mice only containing β5i/LMP7 m20S ([47] and M. Keller, E. Krüger and U. Seifert, unpublished work). Concomitant with i20S, other components of the APM, such as PA28, are up-regulated by IFN-γ [5,12,15]. It was proposed that PA28 might allow the release of slightly longer peptides supporting MHC class I antigen presentation. The influence of PA28 on epitope processing turned out to differ when various epitopes were analysed. Besides the tumour/self-epitope TRP2360–368 (TRP2 is tyrosinase-related protein 2), whose generation is entirely dependent on PA28, there also exist several other examples of epitopes whose generation is improved by PA28 [15,48,49].
Although antigen presentation on infected target cells is an essential prerequisite for rapid recognition and elimination by primed and differentiated CTLs, the dynamics of this process in target cells is still poorly defined. Therefore we have determined the induction kinetics of the immunosubunits and PA28α/β in response to IFNα and IFNγ after 2, 4 and 6 h. It turned out that mRNA expression of all three immunosubunits is induced already after 4 h. To extend our study to other components of the UPS, we investigated the expression of genes related to the UPS in response to type I and type II IFNs in an UPS-focused microarray analysis. Using HeLa cells treated either with IFNγ or IFNα in a time course experiment, it turned out that both IFNγ and IFNα induced more than 20 E3 ligases. These experiments together with the induction of the APM including the i20S subunits and PA28αβ resulted in an unforeseen picture of how IFNs consecutively remodel the UPS at different levels. Thereby the immune responsiveness of target cells is largely improved. The molecular mechanisms of this immune adaptation of the UPS in target cells in these early stages up to 24 h after an immunological challenge remain however to be determined in more detail.
We thank Peter-M. Kloetzel for a critical reading of this paper and helpful discussions. This work was supported by the Deutsche Forschungsgemeinschaft (KR 1915/4–1; SFB421, projects A1 and A11; SFB740, project B3).
Third Intracellular Proteolysis Meeting: A joint Biochemical Society and INPROTEOLYS Network Focused Meeting held at Auditorio de Tenerife, Santa Cruz de Tenerife, Canary Islands, Spain, 5–7 March 2008. Organized and Edited by Rosa Farràs (Centro de Investigación Príncipe Felipe, Valencia, Spain), Gemma Marfany (Barcelona, Spain), Manuel Rodríguez (CICbioGUNE, Derio, Spain), Eduardo Salido (La Laguna, Tenerife, Spain) and Dimitris Xirodimas (Dundee, U.K.).
Abbreviations: APM, antigen presentation machinery; CTL, cytotoxic T-lymphocyte; DUB, deubiquitinating enzyme; ER, endoplasmic reticulum; HCV, hepatitis C virus; i20S, immunoproteasomes; m20S, mixed-type proteasomes; s20S, standard proteasomes; IFN, interferon; LMP, low-molecular-mass protein; MECL1, multicatalytic endopeptidase complex-like 1; NK, cell, natural killer cell; PA28, proteasome activator 28; POMP, proteasome maturation protein; UBL, ubiquitin-like protein; UPS, ubiquitin–proteasome system
- © The Authors Journal compilation © 2008 Biochemical Society


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Posted by City Asia Express in Business | Nov. 25, 2014 | 0 Comments
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|Reviews for Pray
| yseult chapter 1 . 9/27/2008
Loved the flow of this one. Very emotional, very even without being too much. Only thing _I_ would have done differently is the last line. I would have made it shorter for maximum impact. But that's me ;-)
| Pjhoisfhd chapter 1 . 5/14/2007
it's really well-written and emotional. and from what i've read here on fanfic, very original. most angsty fics are completely about trin's death, forgetting the rest of human kind back in zion.
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wow...this is nice...really touching...tho you didn't write on how morpheus thought neo would feel, but nvm :)


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Contact Info / Websites
All 12 audio Reviews
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Rated 4.5 / 5 stars
RAW RAW Fight the powah!
Tea and Crumpets
Rated 3.5 / 5 stars
7/10 - Ahaha wicked!
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Effin' fab.
Loud Whispers w/ Sorohanro
Rated 3.5 / 5 stars
7/10 - Wow...
Loving every minute of it. I can't say anything more... Just... Wow.
What We Are
Rated 4 / 5 stars
8/10 - Spooky! D:
Spookily awesome. Just amazing, dude. Just my cup of tea. ;D
Forever Gamer
Rated 5 / 5 stars
10/10 - Amazing...
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Rated 4 / 5 stars
8/10 - Loving that buildup!
It builds up seamlessly and is all-around amazing. I dunno what more I can say. xD;; Just so amazing.
What is <3
Rated 3.5 / 5 stars
7/10 - Awesome Remix of an Awesome song!
Amazing. I'm a huge fan of the original song. Usually, when I hear a remix I go commit genocide and/or other things of the sorts - but not this... This is smashing.
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Rated 4 / 5 stars
I'm so glad it's not just a couple of minutes long. I could listen to this for hours.
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Rated 5 / 5 stars
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Rated 3.5 / 5 stars
7/10 - Hauntingly Good.
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Most proteins, in order to perform their biological function, have to fold to a compact native state. The increasing number of knotted and slipknotted proteins identified suggests that proteins are able to manoeuvre around topological barriers during folding. In the present article, we review the current progress in elucidating the knotting process in proteins. Although we concentrate on theoretical approaches, where a knotted topology can be unambiguously detected, comparison with experiments is also reviewed. Numerical simulations suggest that the folding process for small knotted proteins is composed of twisted loop formation and then threading by either slipknot geometries or flipping. As the size of the knotted proteins increases, particularly for more deeply threaded termini, the prevalence of traps in the free energy landscape also increases. Thus, in the case of longer knotted and slipknotted proteins, the folding mechanism is probably supported by chaperones. Overall, results imply that knotted proteins can be folded efficiently and survive evolutionary pressure in order to perform their biological functions.
- artificial knot
- chaperone
- free energy landscape
- knotted protein
- protein folding
- slipknotted protein
For a long time, it was believed that knots were too complicated to exist in protein structures [1]. The situation changed in 2000 [2] when the first deeply embedded protein knot was discovered. Since then, knots and slipknots (slipknots arise from threading one loop through another, while the entire chain remains unknotted [3]) have been discovered in 2% of the proteins deposited in the PDB [4–7]. Although this number is significant, it is small in comparison with the ubiquitous knots in globular homopolymers [8,9]. This suggests that protein knots are limited either by the challenges of folding and misfolding or that knots have been systematically discriminated against by Nature for not providing an advantage to the organism [10]. Which case is true is a very intriguing and challenging question.
Recent results show that knotted motifs can be conserved across different families despite very low sequence similarity [11]. This suggests that these knots are conserved to preserve some functional advantage since their complex folding is likely to be disadvantageous for their host organisms. Currently, the functions of knots are not known. However, different types of stabilizing capacities of knots and slipknots have been suggested [7,11–15].
How complicated are protein knotting mechanisms? In the case of unknotted small or midsize proteins, it is known that they fold upon minimally frustrated funnel-like energy landscapes, which allow for fast and robust folding [16,17]. Native contacts play a dominant role in guiding these proteins to their native states in the range of microseconds to seconds. Relatively few complicated folding mechanisms have been proposed; examples are backtracking in interleukin 1β [18,19] or GFP (green fluorescent protein) [19a]. Thus, in principle, the low frequency of knotted proteins may be a consequence of the topological barrier to folding. Proteins that fold too slowly will be eliminated by evolution. Therefore it is important to understand how existing knotted proteins can find their native states. Are there multiple pathways possible for folding knots? Are native contacts [20] always sufficient to fold knotted proteins, and, if not, how are chaperones involved?
Currently, research is focused on three main aspects of knotted proteins: their evolutionary pathway, their tying mechanism and the function of the knotted topology [2,6,7,11,21,22]. In the present review, we summarize our present understanding of the tying process in proteins. Other reviews on the topic of knotted proteins can be found in [7,15,22,23], and, of particular relevance to the present review, the mechanism for untying is discussed in [23].
The folding mechanism of trefoil knotted proteins
The tying process has been most intensely investigated for the proteins YibK, from Haemophilus influenzae, and YbeA, from Escherichia coli [24], members of the SPOUT methyltransferase superfamily that conserve a deeply knotted trefoil at the C-terminus [11]. Recent in vitro results show that both YibK and YbeA can fold spontaneously in approximately 20 min [25]. However, chaperones are shown to significantly accelerate the knotting mechanism. The most important advance in this study was initiating folding from an unknotted and denatured protein since other studies have shown that the knotted topology persists in the denatured state [26] and during mechanical manipulations [12,27,28]. Comparison of folding times between unknotted [25] and knotted-unfolded [26] protein chains suggests that knotting is the rate-limiting step during folding.
Whereas experiments have shown unequivocally that isolated proteins can fold into knots, a structural explanation of the folding process is still beyond experimental resolution. The detailed structural information available in theoretical simulations is shedding considerable light on knotting mechanisms. Before experimental confirmation, it was shown in 2009 that native contacts are able to guide the folding process of YibK and YbeA [29] using SBMs (structure-based models) [20,30]. Their folding process comprises two main steps: a native twisted loop formation and the threading of the shorter terminus via a slipknot conformation (Figure 1). The low success rate (<5%) for reaching the native knotted configuration was explained as a consequence of deep energetic and topological traps. Knot threading was identified as a rate-limiting step for folding in these proteins since an unknotted construct achieved a much higher success rate (~73%). This slipknot folding mechanism was preferred over forming shallow knots that could be converted into native knots. This is surprising in the light of experimental results showing that flexible polymers (strings) can knot spontaneously [31].
Heterogeneous interactions in the knotted region were able to increase the folding rate of YibK [29,32]. It was shown that the slipknot intermediate and the twist (region closing the native knotted loop) is formed by the amino acids glycine (flexible) and proline (stiff). In a homogeneous SBM, these amino acids and all native contacts interact with the same strength. Adding flexibility to glycine, stiffening proline and introducing heterogeneity to the native contact interactions in the knotted region of the SBM increased the successful knotting rate [29,32]. In a different study, introduction of targeted non-native contacts between the C-terminus and the knotted loop significantly decreased the topological barrier and allowed YibK to fold with near 100% efficiency [29,32]. However, these contacts completely change the knotting mechanism from slipknotting to pulling (threading shallow knots). Appropriate interplay between non-native and native contacts can knot proteins even twice the size of YibK, as was observed for AOTCase (aspartate/ornithine carbamoyltransferase) [33].
The predicted tying mechanism (slipknot intermediate) has been seen in other models as well. The potential energy surface of truncated YibK [34] shows that the threading of the terminus through a twisted loop occurs late in the folding process, thereby creating a large energy barrier that serves as the rate-limiting step in the folding process. Interestingly, various unfolding simulations using Cα, all-atom SBM or explicit solvent models all showed that the slipknot conformation is commonly used to untie YibK [35] or AOTCase [14,33]. Folding a trefoil knot (which mimics YibK) on a lattice model [36] showed properties similar to those in a continuous model [29]. These results, along with those presented in the next section, imply that folding knots via slipknots is a robust feature of knotted protein energy landscapes.
The free energy landscape of the two smallest knotted proteins
In 2010, the smallest knotted protein (PDB code 2EFV) was found [37]. The protein 2EFV creates a trefoil knot located at least ten amino acids deep from both termini (Figure 2A). Using an SBM [38] based solely on the native contacts [29,33], 2EFV became the first knotted protein for which a free energy landscape, F(Q) (Figure 2A), was determined [39]. The thermodynamics data revealed an intermediate with twisted loop formation and knot threading at the top of the free energy barrier. The transition state ensemble showed two folding routes: a plugging route and a slipknotting route. We present, as well, new data for VirC2, a protein that has the same fold as 2EFV, but with a deeper knot and only 33% sequence similarity. Figure 2 shows that the two proteins have analogous free energy profiles with clear pre-knotted intermediate states. The analysis shows the dominant effect of topology on the folding route.
Artificial knots through protein design
The first detailed in vitro experimental characterization of equilibrium protein folding/knotting was achieved by designing a novel knotted protein based on genetic fusion of the tandem repeat of a gene of an unknotted dimeric protein [40]. This designed protein reversibly ties itself into the intended natively knotted configuration. Its folding time was shown to be 20-fold slower than that of a twin protein, which was designed to have an analogous tertiary structure, but to be unknotted. This reversibly foldable knotted protein is amenable to simulations, and showed close qualitative and quantitative agreement between experimental and theoretical results, suggesting further that SBMs (and simulations in general) are an important tool for explaining the tying process that is still hidden from experimental resolution. Simulation with SBMs was possible since the native topology was known from X-ray crystallography [40]. Key conclusions from the simulations were that (i) knotting occurs in the transition state ensemble, (ii) kinetics data reflect the experimentally observed rollover in the folding limbs of chevron plots, (iii) correct folding or tying is restricted to a narrow range of temperatures in comparison with the unknotted protein [11], and (iv) the presence of a dead-end intermediate that lacks the knot suggests the importance of backtracking events [41]. Moreover, the results [11] suggest that gene fusion coupled with evolutionary optimization of the stiffness and size of the knotted protein core is a feasible process for creating small knotted proteins that can fold reversibly.
Proteins with complex knotted fingerprints
Identified in 2010, the 61 knot in DehI [37] represents the most complex knot known [11]. Hints of how this protein can fold were obtained from SBM simulations. Even though the folding rate was very low (even lower than for YibK [29]), successful folding trajectories showed a simple tying process. DehI first folds two aligned unknotted loops then ties a knot by (i) threading the C-terminus through the smaller loop (through a slipknot conformation), and (ii) flipping the larger loop over the smaller loop, where the order of the steps (i) and (ii) can be reversed. Flexible regions with glycine and proline are involved in flipping the loop, the twisted arc and the temporary slipknotted configuration.
In 2006, a shallow 52 knot [7] was identified in the UCHs (ubiquitin C-terminal hydrolases) UCH-L1 and UCH-L3, whose function is the degradation of proteins. Available in vitro data on UCHs suggest reversible folding/knotting under chemical denaturation [42]. The kinetics suggest parallel pathways with two intermediate states. Such a landscape is plausible because of the very shallow knot that allows spontaneous knotting through thermal fluctuations after folding the core of the protein. However, verification of an unfolded/unknotted state is still required in order to confirm this interpretation of the kinetic data.
Natively slipknotted proteins [3,11], although untied when pulled from their termini [43,44], create a very interesting class of proteins with non-trivial folding processes. Currently, it is known that several slipknots in tandem can create complex knotted motifs that are conserved despite low sequence similarity [3,11]. Results suggest a reversible unfolding and folding process composed of multiple routes for alkaline phosphatase, a protein with a simple slipknot motif [3,11]. SBM simulations of a protein with the same slipknot motif, thymidine kinase, explained the folding process by a 'flipping mechanism', in which the slipknot formation is initiated by rotation of the slip-loop over the unknotted native core of the protein [29]. Glycine and proline are found in the hinge regions that probably support this rotation. The flipping mechanism represents the simplest way to fold a slipknot; however, the small number of successful folding events suggests participation of external help to overcome deep topological traps.
Analogous knotting mechanisms for other complex knotted proteins were suggested by considering sequence and knotted motif conservation [3,11]. It was shown that families with a conserved knotted fingerprint, despite having low sequence similarity, show a preference for the conservation of glycine in the hinge regions. These amino acids can facilitate folding and suggest a knotting mechanism composed of the steps observed in smaller proteins. Much shorter slipknotted proteins, such as those encoded by crenarchaeal virus AFV3 (Acidianus filamentous virus 3) open reading frame 109, fold employing only the first three steps in Figure 1 [29]. This provides strong support for a common knotting process between knotted and slipknotted proteins.
In summary, numerical simulations suggest a set of related folding mechanisms for knotted proteins. It consists of twisted loop formation, and then threading by either slipknot configurations or flipping motions. This general knotting mechanism is robust across all knotted or slipknotted protein topologies that can be untied in one step (which is the case for all known proteins) as suggested in [22]. Combination of experimental and theoretical results shows that small knotted proteins can be reversibly self-tied, whereas proteins with deep or complex knots may need some external guidance to fold, for example from chaperones [25]. The precise action of these chaperones remains unknown, but their general role would be to enable protein conformations to overcome topological traps and to facilitate the proposed folding mechanisms. In the future, detailed methods such as single-molecule fluorescence need to be incorporated into in vitro studies in order to strengthen the combined experimental and theoretical efforts to elucidate the driving force for tying knots in proteins.
J.I.S., J.K.N. and J.N.O. were supported by the Center for Theoretical Biological Physics sponsored by the National Science Foundation (NSF) [grant numbers PHY-0822283 and MCB-1214457]. J.N.O. is a Cancer Prevention and Research Institute of Texas (CPRIT) Scholar in Cancer Research sponsored by CPRIT. J.I.S. was supported by the Fundacja na rzecz Nauki Polskiej (FNP) and the Foundation for Polish Science TEAM Project [grant number TEAM/2011-7/6]. E.J.R. was supported by the National Science Foundation [grant number 1115722]. C.A.R.-S. was supported by a Comisión Nacional de Investigación Científica y Tecnológica (CONICYT) doctoral fellowship.
J.I.S., E.J.R. and K.C.M. thank the Isaac Newton Institute for Mathematical Sciences for sponsoring the Topological Aspects of DNA Function and Protein Folding workshop and for hosting our stays at the Institute.
Topological Aspects of DNA Function and Protein Folding: An Independent Meeting held at the Isaac Newton Institute for Mathematical Sciences, Cambridge, U.K., 3–7 September 2012, as part of the Isaac Newton Institute Programme Topological Dynamics in the Physical and Biological Sciences (16 July–21 December 2012). Organized and Edited by Andrew Bates (University of Liverpool, U.K.), Dorothy Buck (Imperial College London, U.K.), Sarah Harris (University of Leeds, U.K.), Andrzej Stasiak (University of Lausanne, Switzerland) and De Witt Sumners (Florida State University, U.S.A.).
Abbreviations: AOTCase, aspartate/ornithine carbamoyltransferase; SBM, structure-based model; UCH, ubiquitin C-terminal hydrolase
- © The Authors Journal compilation © 2013 Biochemical Society


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Nedley's Depression/Anxiety Recovery Program
Dec 4, 2016 | by Lisa Reynoso
It's the most wonderful time of the year…. At least it's supposed to be. Maybe having loved ones and family around is helping with the blues but what happens when they all go home?
Did you know that approximately 121 million people around the world suffer from some form of depression? America has one of the highest percentages of Major Depressive Episodes!
Are you tired of being that statistic or fighting to overcome it?
We will be hosting Dr. Nedley's Depression and Anxiety Recovery Program locally just for you. Join us on January 3rd at 7:00pm for the introductory session and see for yourself the results you can achieve by trying a few new things.
Location: Tremont Evangelical Church, 7115 SE Woodstock Blvd, Portland, OR 97206
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text: Judith Duncan from Canterbury University has led a 2-year research project with Central Baptist Kindergarten in Whanganui on participation and developing community around their centre. This work has been made into a series of videos, one of which is embedded here for a taster. A fantastic locally-made resource, these videos are all well worth viewing!


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text: Essay-based examinations are common in many subjects. The writing skills you need to do well in this type of exam are similar to those needed for writing coursework essays, but the situation is very different: in an essay exam, you have to write on an unseen topic under timed conditions. This makes many students anxious about their ability to do well in exams. If you are one of them, these pages will help. They contain information and advice on how to prepare for essay exams, how to tackle the exam paper and how to answer the questions.


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Housing blocks must be assessed
More than 100 Christchurch housing blocks and units must be assessed by engineers to determine if they are earthquake-prone.
However, property managers say a shortage of engineers could create a backlog of up to 18 months.
The Canterbury Earthquake Recovery Authority (Cera) confirmed yesterday that 114 residential properties requiring detailed engineering evaluations (DEEs) were "in the system".
All commercial buildings and residential buildings of two or more storeys and containing three or more household units needed to be assessed, but other residential buildings were exempt.
Some of the 114 properties listed were individual units within multi-storey buildings and others were multi-unit buildings.
Tony Brazier, of Brazier Property Investments, said clients had begun receiving DEE letters from Cera, but no assessments had been undertaken.
"The hard part is finding an engineer in the next six to 18 months who's got time to do it," he said. "I've gone from one engineer to another to try to get a speedier approach on my own commercial building, and you really just can't hurry anyone, and maybe we shouldn't."
Property owners believed the DEEs were a "necessary evil", Brazier said.
Evaluation cost estimates were between $3000 and $18,000.
"[Owners] don't particularly like it because a lot of the flats, especially the multi-level flats that are multi-unit, have been some of the best properties to survive through the earthquakes," he said.
"I've got several blocks of flats and really [damage] has been minor, so to spend thousands of dollars to get a DEE . . . Nobody's looking forward to it."
Commercial evaluations should be completed first and then residential properties, Brazier said.
Tenants queried the safety of some properties immediately after the February 2011 quake, but there had been few complaints since, he said.
Martin Evans, of A1 Property Managers, said none of his clients had been asked to supply DEEs. Builders and engineers had inspected every property his company managed. "If we have a tenant who is concerned, we send an engineer out to have a look at it, or a builder for a start."
A Cera spokeswoman said the standard DEE time frame was eight weeks, but the approach was "realistic and flexible".
The Press