Synthesis, Assembly and Function of the E. Coli H+-ATPase
{'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 research will investigate 3 aspects of the synthesis and                    assembly of the E.coli enzyme.  1) It has been shown that                       certain F1 subunits actually open the Fo proton channel.  By                    cloning ATPase genes in various combinations, and by                            constructing various truncated and mutant subunits, it will                     demonstrate exactly which subunits, and which regions of                        those subunits, are responsible for enhancing proton                            conduction through the Fo 2) It has been shown that a change                    in gene expression can produce an ATPase with altered                           energy-coupling characteristics.  The different ATPases will                    be purified and reconstituted to demonstrate what those                         structural changes are and what effects they have on the                        enzyme's activity.  3) ATPase subunits are differentially                       synthesized and then assembled.  It will then be determined                     to what extent newly synthesized subunits are degraded by                       proteases in vivo and how they might be protected from such                     proteases during assembly by binding to other subunits.                                                                                                         Proton translocating ATPase are large multimeric, membrane-                     bound enzymes which, acting as ATP in biological systems.                       They are therefore at the heart of energy metabolism and are                    central to any discussion or study of biological energy                         coupling.  These enzymes catalyze a reaction whose mechanism                    is unknown - they couple the movement of protons across a                       membrane to the synthesis or hydrolysis of ATP.  In bacteria,                   plants and animals they use the proton motive generated by                      oxidative electron transport or photosynthetic oxygenic                         electron transport to synthesize ATP from ADP and Pi.  The                      ATP synthase in E. coli can synthesize ATP, and also can act                    as an ATPase.  It is freely reversible in vivo in contrast to                   the eukaryotic enzyme.  It is hoped to answer an as yet,                        unanswered question, how does energy coupling occur.  Dr.                       Busilow has a very unique approach to explore this problem                      and is well prepared to carry out this study.
{'FirstName': 'William', 'LastName': 'Brusilow', 'PI_MID_INIT': 'S', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'William S Brusilow', 'EmailAddress': None, 'NSF_ID': '000236683', 'StartDate': '08/15/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Maryland, College Park', 'CityName': 'COLLEGE PARK', 'ZipCode': '207425100', 'PhoneNumber': '3014056269', 'StreetAddress': '3112 LEE BUILDING', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Maryland', 'StateCode': 'MD', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'MD04', 'ORG_UEI_NUM': 'NPU8ULVAAS23', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF MARYLAND, COLLEGE PARK', 'ORG_PRNT_UEI_NUM': 'NPU8ULVAAS23'}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8805416.xml'}