Function of Subunit Isologs in Cytochrome c Oxidase
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Eve Ida Barak', 'PO_EMAI': None, 'PO_PHON': None}
The recent discovery of isologs to the nuclear-coded subunits                   of cytochrome c oxidase has led to the hypothesis that these                    polypeptides play a role in the modulation of cytochrome c                      oxidase activity and that this modulation is affected by a                      differential expression of their genes in response to                           environmental (or developmental) signals.  This hypothesis will                 be tested by studying the two isologs Va and Vb for subunit V                   of yeast cytochrome c oxidase.  Preliminary studies have                        suggested that mutant cells carrying only Vb produce cytochrome                 c oxidase molecules whose in situ turnover numbers are higher                   than those produced in mutant cells carrying only Va.  The                      effects of Va and Vb on the binuclear reaction center in                        holocytochrome c oxidase and the interactions of the enzyme                     with its substrates oxygen and cytochrome c will be examined.                   Do the holoenzymes that carry Va or Vb interact preferentially                  with one of the two cytochrome c isologs?  An answer will be                    sought.  Chimeric proteins will be contructed and the domains                   in Va and Vb that modulate the catalytic functions of the                       enzyme will be identified and located with respect to the inner                 mitochondrial membrane.  How does intracellular levels of Va                    and Vb change in response to cell physiology?                                                                                                                   Cellular energy production is necessary for the growth and                      division of cells and cytochrome c oxidase is a key component                   in the respiratory chain, a multienzyme complex.  Mitochondrial                 oxidative phosphoylation is capable of supplying more than 95%                  of the total ATP requirement in respiring encaryotic cells.                     The respiratory chain that drives it acts in series to affect                   the transfer of electrons from reduced substrates to water.                     Cytochrome c is the terminal member of this chain and seems to                  be the key enzyme in cellular energy production.  It is very                    important to discover how eukaryotic cells alter their                          cytochrome c oxidase activity levels in response to energy                      demand.  Dr. Poyton has done very significant work in this                      field and is certainly well suited to carry out this                            investigation.
{'FirstName': 'Robert', 'LastName': 'Poyton', 'PI_MID_INIT': 'O', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Robert O Poyton', 'EmailAddress': None, 'NSF_ID': '000110699', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Colorado at Boulder', 'CityName': 'Boulder', 'ZipCode': '803090001', 'PhoneNumber': '3034926221', 'StreetAddress': '3100 MARINE ST', 'StreetAddress2': 'STE 481 572 UCB', 'CountryName': 'United States', 'StateName': 'Colorado', 'StateCode': 'CO', 'CONGRESSDISTRICT': '02', 'CONGRESS_DISTRICT_ORG': 'CO02', 'ORG_UEI_NUM': 'SPVKK1RC2MZ3', 'ORG_LGL_BUS_NAME': 'THE REGENTS OF THE UNIVERSITY OF COLORADO', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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