Reconstitution of DNA Polymerase Holoenzyme
{'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 overall goal of this project is to elucidate the                            structure, function and regulation of the mammalian                             replication complex.  The focus of the work will be DNA                         polymerase delta, the only mammalian DNA polymerase with                        intrinsic 3' - 5' exonuclease activity capable of correcting                    errors of incorporation.                                                                                                                                        The major thrust of this project is to identify, purify and                     characterize the subunits of DNA polymerase delta holoenzyme                    and other accessory proteins that are part of this                              multiprotein complex, which may function as a replication                       apparatus in mammalian cells.  Another objective is to                          reconstitute active replication complexes from purified                         components.  Several strategies wil be employed, including                      protein affinity and immunoaffinity chromatography, to                          identify and purify components of the replication complex.                      Cloned cDNAs which encode DNA polymerase delta holoenzyme                       subunits or accessory proteins will also be prepared as                         additional tools to investigate the structure, function and                     regulation of the mammalian replication complex.                                                                                                                Previous work has resulted in the identification and                            purification to homogeneity of an auxillary protein for DNA                     polymerase delta which enables the core enzyme to utilize                       template/primers containing long stretches of single stranded                   template.  Thus it is now possible to investigate the effects                   of putative replication complex components on the efficiency,                   processivity and fidelity with which DNA polymerase delta                       replicates primed natural DNA templates.
{'FirstName': 'Antero', 'LastName': 'So', 'PI_MID_INIT': 'G', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Antero G So', 'EmailAddress': None, 'NSF_ID': '000283786', 'StartDate': '10/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Miami School of Medicine', 'CityName': 'CORAL GABLES', 'ZipCode': '331462926', 'PhoneNumber': '3052843924', 'StreetAddress': '1320 S DIXIE HWY STE 1200', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Florida', 'StateCode': 'FL', 'CONGRESSDISTRICT': '27', 'CONGRESS_DISTRICT_ORG': 'FL27', 'ORG_UEI_NUM': 'F8THLJQSAF93', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF MIAMI', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1144', 'Text': 'Molecular Biophysics'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8703747.xml'}