Studies of Ribonuclease P (RNase P)
{'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 structural features of the catalytic RNA subunit and                        the protein subunit of RNAase P from E. coli, which are                         required for catalysis and the accurate cleavage of tRNA                        precursor molecules, will be investigated by utilizing subunits                 of enzyme that have been altered by chemical enzymatic or                       genetic methods.  Derivatives of the catalytic subunit or                       altered forms of the RNase P holoenzyme with Km or k cat                        values,  different from those of the wild type will be                          identified.  In  particular, subunits of the enzyme, in                         combination with  modified substrates, will be used to improve                  the yield of  enzyme-substrate complexes, and thereby                           facilitate the identification and study by chemical techniques                  of the active site of the enzyme.  Model substrates will be                     synthesized to determine the features of the substrates which                   are essential for cleavage by the enzyme.  Hybrid enzymes,                      composed of subunits from different organisms, will also be                     used to determine the role played by each subunit in the                        catalytic activity of the holoenzyme in vitro.  Attempts to                     crystallize the RNase P from E. coli will proceed concurrently.                                                                                                 The importance of the processing of RNA in the  biosynthesis of                 RNA molecules and in the regulation of gene  expression during                  the cell cycle of simple organisms and during differentiation                   of higher organisms is well established.  It is apparent that                   the endo and exonucleolytic cleavages, ligations, modification                  and addition of nucleotides, which RNA molecules undergo are                    not biochemical curiosities, but are essential to the normal                    function and expression of all genomes.  Many of these                          reactions involve novel mechanisms of catalysis and/or novel                    aggregates of macromolecules which either directly govern                       processing reactions or in some way act as cofactors.  Dr.                      Altman originally discovered that RNA is an essential component                 of RWase P.  After the discovering of self-splicing introns he                  showed that RNA above could perform the catalytic function.
{'FirstName': 'Sidney', 'LastName': 'Altman', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Sidney Altman', 'EmailAddress': 'sidney.altman@yale.edu', 'NSF_ID': '000125150', 'StartDate': '07/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Yale University', 'CityName': 'NEW HAVEN', 'ZipCode': '065113572', 'PhoneNumber': '2037854689', 'StreetAddress': '150 MUNSON ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Connecticut', 'StateCode': 'CT', 'CONGRESSDISTRICT': '03', 'CONGRESS_DISTRICT_ORG': 'CT03', 'ORG_UEI_NUM': 'FL6GV84CKN57', 'ORG_LGL_BUS_NAME': 'YALE UNIV', 'ORG_PRNT_UEI_NUM': 'FL6GV84CKN57'}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8722644.xml'}