Protein Export in Bacteria
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'M.  Paige', 'PO_EMAI': None, 'PO_PHON': None}
The long-term objective is understanding the mechanism by which                 proteins cross through membranes.  The proposed research is a                   biochemical characterization of the energy requirements for                     protein transport across the Escherichia coli inner membrane.                                                                                                   An established, in vitro, bacterial protein export assay will be                used to measure the effects of both ATP and a transmembrane                     electrochemical potential on protein export.  The in vitro assay                allows these energy sources to be carefully controlled and                      measured during the movement of proteins across inner membrane                  vesicles.  Previous results have shown that both ATP and an                     electrochemical potential are necessary for protein export in                   vitro.  By sequentially adding ATP and a transmembrane                          electrochemical potential to the in vitro assay, the order and                  timing of the energy requirements can be understood with respect                to the individual molecular steps that occur during this complex                reaction.                                                                                                                                                       The requirement for ATP, independent of the electrochemical                     potential, suggests that ATP hydrolysis may be necessary for                    protein export.  Preliminary evidence indicates that during                     protein export, the terminal phosphate residue of ATP is                        transferred to a cellular component with an apparent size of                    about 30,000 daltons.  The effects of inhibitors of protein                     export on this phosphate group transfer will be measured.  A                    correlation between the extent of inhibition of protein export                  and phosphate transfer would further define the role of ATP in                  protein export.  The phosphate label may allow a means of                       isolating this potentially important component in protein export.
{'FirstName': 'Bruce', 'LastName': 'Geller', 'PI_MID_INIT': 'L', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Bruce L Geller', 'EmailAddress': 'GELLERB@CCMAIL.ORST.EDU                 503-737-0496 FAX', 'NSF_ID': '000329375', 'StartDate': '07/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Oregon State University', 'CityName': 'CORVALLIS', 'ZipCode': '973318655', 'PhoneNumber': '5417374933', 'StreetAddress': '1500 SW JEFFERSON AVE', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Oregon', 'StateCode': 'OR', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'OR04', 'ORG_UEI_NUM': 'MZ4DYXE1SL98', 'ORG_LGL_BUS_NAME': 'OREGON STATE UNIVERSITY', '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=1986&All=true', 'xml': '8618186.xml'}