Mutational Analysis of the Biological Function of HMG       Proteins
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Marcia Steinberg', 'PO_EMAI': None, 'PO_PHON': None}
The role of the histones in chromatin structure is                         understood, but the function of most non-histone, chromatin-                    associated proteins, including the intensively investigated                     HMG (High Mobility Group) proteins, is unclear.  We have                        cloned the genes for several HMG-like proteins from the yeast                   Saccharomyces cerevisiae, thus affording us the opportunity                     to use a combination of genetic and biochemical approaches to                   determine, for the first time, the biological function for                      chromatin-associated HMG-like proteins.                                              To generate conditionally lethal mutations in the                          HMG-like proteins, cellular HMG-like genes will be replaced                     with cloned HMG-like genes mutagenized in vitro.  All of the                    mutants will be biochemically analyzed for changes in RNA,                      DNA and protein synthesis as well as for changes in chromatin                   structure.  The results of these experiments will define the                    in vivo function of each HMG-like protein.                                           A future direction of this research is in vitro studies                    of the mechanisms of HMG-like protein function using the wild                   type and mutant proteins.  Thus, a non-denaturing                               purification scheme using chromatographic procedures,                           including immunoaffinity columns, will be developed.                            Finally, to begin to establish the interactions of HMG-like                     proteins with other chromatin proteins, extragenic                              suppressors of the mutants in HMG-like proteins will be                         isolated.                                                                            The proposed experiments will increase our comprehension                   of the eukaryotic chromosome.
{'FirstName': 'David', 'LastName': 'Kolodrubetz', 'PI_MID_INIT': 'J', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'David J Kolodrubetz', 'EmailAddress': '5125673967', 'NSF_ID': '000231427', 'StartDate': '04/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Texas Health Science Center San Antonio', 'CityName': 'SAN ANTONIO', 'ZipCode': '782293901', 'PhoneNumber': '2105672340', 'StreetAddress': '7703 FLOYD CURL DR', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Texas', 'StateCode': 'TX', 'CONGRESSDISTRICT': '20', 'CONGRESS_DISTRICT_ORG': 'TX20', 'ORG_UEI_NUM': 'C3KXNLTAAY98', 'ORG_LGL_BUS_NAME': 'THE UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8718632.xml'}