Cooperative Binding of 434 Phage Repressor
{'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 repressor of the E.coli bacteriophage 434 is similiar in                    overall structure to lambda repressor and, like lambda                          repressor, it binds cooperatively to adjacent operator sites                    on DNA.  Unlike lambda repressor, however, 434 repressor does                   not bind cooperatively to separated sites on DNA as assayed                     in vitro.  The objective of this proposal is to investigate                     the basis of this difference in an array of experiments.                                                                                                        Genetically engineered 434-lambda repressor hybrids will be                     generated and studied in order to determine the basis of the                    observed differences in the abilities of 434 and lambda                         repressor to bind cooperatively to nonadjacent operator                         sites.  A system for studying cooperatively "at a distance"                     in vivo using 434 operators will be established.  This system                   will be used to detect and investigate hybrid and mutant                        repressors.  Efforts will be made to ascertain whether                          specific "DNA-bending" sequences in the OL region of the                        phage allow 434 repressor to bind cooperatively to                              nonadjacent sites.                                                                                                                                              These studies should provide new insight into those aspects                     of protein structure necessary for interaction of DNA-bound                     regulatory proteins "at a distance".
{'FirstName': 'Mark', 'LastName': 'Ptashne', 'PI_MID_INIT': 'S', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Mark S Ptashne', 'EmailAddress': None, 'NSF_ID': '000380346', 'StartDate': '08/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Harvard University', 'CityName': 'CAMBRIDGE', 'ZipCode': '021385366', 'PhoneNumber': '6174955501', 'StreetAddress': '1033 MASSACHUSETTS AVE STE 3', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Massachusetts', 'StateCode': 'MA', 'CONGRESSDISTRICT': '05', 'CONGRESS_DISTRICT_ORG': 'MA05', 'ORG_UEI_NUM': 'LN53LCFJFL45', 'ORG_LGL_BUS_NAME': 'PRESIDENT AND FELLOWS OF HARVARD COLLEGE', 'ORG_PRNT_UEI_NUM': None}
{'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': '8704264.xml'}