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bionlp2004

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16600
Activation of the HIV-1 enhancer by the LEF-1 HMG protein on nucleosome-assembled DNA in vitro .
Activation of the <dna>HIV-1 enhancer</dna> by the <protein>LEF-1 HMG protein</protein> on <dna>nucleosome-assembled DNA</dna> in vitro .
16601
Lymphoid enhancer-binding factor 1 ( LEF-1 ) is a regulatory high mobility group ( HMG ) protein that activates the T cell receptor alpha ( TCR alpha ) enhancer in a context-restricted manner in T cells .
<protein>Lymphoid enhancer-binding factor 1</protein> ( <protein>LEF-1</protein> ) is a <protein>regulatory high mobility group ( HMG ) protein</protein> that activates the <dna>T cell receptor alpha ( TCR alpha ) enhancer</dna> in a context-restricted manner in <cell_type>T cells</cell_type> .
16602
In this paper we demonstrate that the distal region of the human immunodeficiency virus-1 ( HIV-1 ) enhancer , which contains DNA-binding sites for LEF-1 and Ets-1 , also provides a functional context for activation by LEF-1 .
In this paper we demonstrate that the distal region of the <dna>human immunodeficiency virus-1 ( HIV-1 ) enhancer</dna> , which contains <dna>DNA-binding sites</dna> for <protein>LEF-1</protein> and Ets-1 , also provides a functional context for activation by <protein>LEF-1</protein> .
16603
First , we show that mutations in the LEF-1-binding site inhibit the activity of multimerized copies of the HIV-1 enhancer in Jurkat T cells , and that LEF-1/GAL4 can activate a GAL4-substituted HIV-1 enhancer 80- to 100-fold in vivo .
First , we show that mutations in the <dna>LEF-1-binding site</dna> inhibit the activity of <dna>multimerized copies</dna> of the <dna>HIV-1 enhancer</dna> in <cell_line>Jurkat T cells</cell_line> , and that <protein>LEF-1/GAL4</protein> can activate a <dna>GAL4-substituted HIV-1 enhancer</dna> 80- to 100-fold in vivo .
16604
Second , recombinant LEF-1 is shown to activate HIV-1 transcription on chromatin-assembled DNA in vitro .
Second , <protein>recombinant LEF-1</protein> is shown to activate HIV-1 transcription on <dna>chromatin-assembled DNA</dna> in vitro .
16605
By using a nucleosome -assembly system derived from Drosophila embryos , we find that the packaging of DNA into chromatin in vitro strongly represses HIV-1 transcription and that repression can be counteracted efficiently by preincubation of the DNA with LEF-1 ( or LEF-1 and Ets-1 ) supplemented with fractions containing the promoter-binding protein , Sp1 .
By using a <protein>nucleosome</protein> -assembly system derived from Drosophila embryos , we find that the packaging of DNA into <dna>chromatin</dna> in vitro strongly represses HIV-1 transcription and that repression can be counteracted efficiently by preincubation of the DNA with <protein>LEF-1</protein> ( or <protein>LEF-1</protein> and <protein>Ets-1</protein> ) supplemented with fractions containing the <protein>promoter-binding protein</protein> , <protein>Sp1</protein> .
16606
Addition of TFE-3 , which binds to an E-box motif upstream of the LEF-1 and Ets-1 sites , further augments transcription in this system .
Addition of <protein>TFE-3</protein> , which binds to an <dna>E-box motif</dna> upstream of the <dna>LEF-1 and Ets-1 sites</dna> , further augments transcription in this system .
16607
Individually or collectively , none of the three enhancer-binding proteins ( LEF-1 , Ets-1 , and TFE-3 ) could activate transcription in the absence of Sp1 .
Individually or collectively , none of the three <protein>enhancer-binding proteins</protein> ( <protein>LEF-1</protein> , <protein>Ets-1</protein> , and <protein>TFE-3</protein> ) could activate transcription in the absence of <protein>Sp1</protein> .
16608
A truncation mutant of LEF-1 ( HMG-88 ) , which contains the HMG box but lacks the trans-activation domain , did not activate transcription from nucleosomal DNA , indicating that bending of DNA by the HMG domain is not sufficient to activate transcription in vitro .
A <protein>truncation mutant</protein> of <protein>LEF-1</protein> ( <protein>HMG-88</protein> ) , which contains the <protein>HMG box</protein> but lacks the <protein>trans-activation domain</protein> , did not activate transcription from <dna>nucleosomal DNA</dna> , indicating that bending of DNA by the <protein>HMG domain</protein> is not sufficient to activate transcription in vitro .
16609
We conclude that transcription activation by LEF-1 in vitro is a chromatin -dependent process that requires a functional trans-activation domain in addition to the HMG domain .
We conclude that transcription activation by <protein>LEF-1</protein> in vitro is a <dna>chromatin</dna> -dependent process that requires a functional <protein>trans-activation domain</protein> in addition to the <protein>HMG domain</protein> .
16610
HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells [ published erratum appears in J Biol Chem 1995 Dec 1 ; 270 ( 48 ) : 29038 ]
<protein>HIV-1 envelope glycoproteins</protein> induce activation of activated <protein>protein-1</protein> in <cell_type>CD4+ T cells</cell_type> [ published erratum appears in J Biol Chem 1995 Dec 1 ; 270 ( 48 ) : 29038 ]
16611
Activation of CD4 positive T cells is a primary requirement for human immunodeficiency virus ( HIV ) entry , efficient HIV replication , and progression to AIDS , Utilizing CD4 positive T cell lines and purified T cells from normal individuals , we have demonstrated that native envelope glycoproteins of HIV , gp 160 , can induce activation of transcription factor , activated protein-1 ( AP-1 ) .
Activation of <cell_type>CD4 positive T cells</cell_type> is a primary requirement for human immunodeficiency virus ( HIV ) entry , efficient HIV replication , and progression to AIDS , Utilizing <cell_line>CD4 positive T cell lines</cell_line> and <cell_type>purified T cells</cell_type> from normal individuals , we have demonstrated that <protein>native envelope glycoproteins</protein> of HIV , <protein>gp 160</protein> , can induce activation of <protein>transcription factor , activated protein-1</protein> ( <protein>AP-1</protein> ) .
16612
The stimulatory effects of gp160 are mediated through the CD4 molecule , since treatment of gp160 with soluble CD4-IgG abrogates its activity , and CD4 negative T cell lines fail to be stimulated with gp160 .
The stimulatory effects of <protein>gp160</protein> are mediated through the <protein>CD4 molecule</protein> , since treatment of <protein>gp160</protein> with soluble <protein>CD4-IgG</protein> abrogates its activity , and <cell_line>CD4 negative T cell lines</cell_line> fail to be stimulated with <protein>gp160</protein> .
16613
Immunoprecipitation of the gp 160 -induced nuclear extracts with polyclonal antibodies to Fos and Jun proteins indicates that AP-1 complex is comprised of members of these family of proteins .
Immunoprecipitation of the <protein>gp 160</protein> -induced nuclear extracts with <protein>polyclonal antibodies</protein> to <protein>Fos</protein> and <protein>Jun proteins</protein> indicates that <protein>AP-1 complex</protein> is comprised of members of these family of proteins .
16614
The gp160-induced AP-1 complex is dependent upon protein tyrosine phosphorylation and is protein synthesis-independent .
The <protein>gp160-induced AP-1 complex</protein> is dependent upon protein tyrosine phosphorylation and is protein synthesis-independent .
16615
This stimulation can also be abolished by inhibitors of protein kinase C , but it is unaffected by calcium channel blocker or cyclosporine A .
This stimulation can also be abolished by inhibitors of <protein>protein kinase C</protein> , but it is unaffected by calcium channel blocker or cyclosporine A .
16616
This gp160 treatment adversely affects the functional capabilities of T cells : pre-treatment of CD4+ T cells with gp160 for 4 h at 37 degrees C inhibited anti-CD3 -induced interleukin-2 secretion .
This <protein>gp160</protein> treatment adversely affects the functional capabilities of <cell_type>T cells</cell_type> : pre-treatment of <cell_type>CD4+ T cells</cell_type> with <protein>gp160</protein> for 4 h at 37 degrees C inhibited <protein>anti-CD3</protein> -induced <protein>interleukin-2</protein> secretion .
16617
Effects similar to gp160 were seen with anti-CD4 mAb .
Effects similar to <protein>gp160</protein> were seen with <protein>anti-CD4 mAb</protein> .
16618
The aberrant activation of AP-1 by gp160 in CD4 positive T cells could result in up-regulation of cytokines containing AP-1 sites , e.g . interleukin-3 and granulocyte macrophage colony-stimulating factor , and concurrently lead to T cell unresponsiveness by inhibiting interleukin-2 secretion .
The aberrant activation of <protein>AP-1</protein> by <protein>gp160</protein> in <cell_type>CD4 positive T cells</cell_type> could result in up-regulation of <protein>cytokines</protein> containing <dna>AP-1 sites</dna> , e.g . <protein>interleukin-3</protein> and <protein>granulocyte macrophage colony-stimulating factor</protein> , and concurrently lead to <cell_type>T cell</cell_type> unresponsiveness by inhibiting <protein>interleukin-2</protein> secretion .