Biochemistry of Fatty Acid Uptake in Escherichia Coli
{'Code': '08070600', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Maryanna P. Henkart', 'PO_EMAI': None, 'PO_PHON': None}
Long-chain fatty acids (LCFA) traverse the cell envelope of Escherichia         coli by a high-affinity, saturable, energy-dependent process.  This             uptake system requires the functional activities of at least two genes,         fadL and fadD, so that LCFA can be used as a sole carbon and energy             source.  The fadL gene codes for an outer membrane-bound long-chain             fatty acid binding protein, FadL, that is required for the transport of         LCFAs into the cell.  The fadD gene codes for acyl CoA synthetase, an           enzyme presumed to be associated with the inner membrane.                                                                                                       The kinetics of LCFA binding to whole cells blocked for fatty acid              utilization will be determined in an effort to further define the role          of FadL.  In particular, the temperature, pH optima, and fatty acid             chain length specificity of fatty acid binding will be determined.  The         cloned fadL+ gene will be mutagenized in vitro using hydroxylamine and          in vivo by cycling through mutator strains to generate mutants in fadL          that will be used in defining the functional domains of FadL.  The              fatty acid binding domains will be identified using affinity-labelled           LCFAs coupled with peptide sequencing.  Collectively, the data                  generated from this project will be used to develop a model correlating         the functional domains of FadL with the linear amino acid sequence.             In more broad terms, the information gleaned from these experiments             will provide information describing the molecular basis of protein-             fatty acid interaction at the cell surface.  This description,                  therefore, may be applied to more complex cell types in evaluating how          fatty acids traverse the membrane.
{'FirstName': 'Paul', 'LastName': 'Black', 'PI_MID_INIT': 'N', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Paul N Black', 'EmailAddress': 'pblack@ordwayresearch.org', 'NSF_ID': '000418700', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'The University of Tennessee, Memphis - The Health Science Center', 'CityName': 'MEMPHIS', 'ZipCode': '381034902', 'PhoneNumber': '9014484889', 'StreetAddress': '62 S DUNLAP ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Tennessee', 'StateCode': 'TN', 'CONGRESSDISTRICT': '09', 'CONGRESS_DISTRICT_ORG': 'TN09', 'ORG_UEI_NUM': 'X1M1PN3KG3E7', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF TENNESSEE', 'ORG_PRNT_UEI_NUM': 'JBG7T7RXQ2B7'}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '1114', 'Text': 'Cellular Dynamics and Function'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8811714.xml'}