Collaborative Research on the Molecular Functions of the    Signal Sequence in Protein Export
{'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}
This is part of a collaborative project between a bacterial                geneticist (Dr. Silhavy) and a physical chemist (Dr. Gierasch) to               study the molecular functions of the signal sequence in protein                 export.      Most exported proteins are synthesized initially in                precursor form with an amino-terminal signal sequence.                          Convincing evidence demonstrating the essential role of this                    sequence in the export process has been presented.  However,                    details of its function(s) are not well understood.  Because of                 its small size (15-30 amino acids), this export signal is                       particularly amenable to analysis using modern genetic and                      physical techniques, such as gene fusions that specify hybrid                   proteins, site-specific mutagenesis using synthetic                             oligonucleotides, solid-state peptide synthesis, and fluorescence               energy transfer and quenching in model membrane systems.                        Previous results from the laboratories of these researchers                     demonstrated that intrinsic physical-chemical properties of the                 signal sequence are correlated with its in vivo function.  This                 project will expand and amplify the ongoing interdisciplinary                   approach to dissect the molecular mechanism by which the signal                 sequence of exported proteins interacts with a biological                       membrane.  This goal will be facilitated through the use of                     export-defective mutant strains of E. coli in which the signal                  sequence of the outer membrane protein, LamB, is altered, and                   through the physical-chemical study of corresponding synthetic                  signal peptides.
{'FirstName': 'Thomas', 'LastName': 'Silhavy', 'PI_MID_INIT': 'J', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Thomas J Silhavy', 'EmailAddress': 'tsilhavy@princeton.edu', 'NSF_ID': '000282258', 'StartDate': '08/15/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Princeton University', 'CityName': 'PRINCETON', 'ZipCode': '085442001', 'PhoneNumber': '6092583090', 'StreetAddress': '1 NASSAU HALL', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'New Jersey', 'StateCode': 'NJ', 'CONGRESSDISTRICT': '12', 'CONGRESS_DISTRICT_ORG': 'NJ12', 'ORG_UEI_NUM': 'NJ1YPQXQG7U5', 'ORG_LGL_BUS_NAME': 'THE TRUSTEES OF PRINCETON UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1114', 'Text': 'Cellular Dynamics and Function'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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