Export of Outer Membrane Proteins
{'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}
Blocking the later stages of the pathway for the export of                      outer membrane proteins by E. coli leads to an inhibition of                    expression of these proteins which appears to be at the level                   of translation.  This appears to be coupled to the later stages                 of export.  These later stages will be studied in three ways.                   First, using oligonucleotide-directed mutagenesis mutations                     will be introduced into a C-terminal region of the OmpC porin                   protein which has been identified as a site of trans-dominant                   mutations which blocks export.  The effects of these mutations                  on secretion, protein folding and oligomer stability will be                    examined.  Attempts will be made to set up an in vitro system                   for folding and trimerization of OmpC protein using protein and                 LPS precursors which approximate thos found in vivo.  This                      should allow additional study of mutant proteins, and can be                    used to study protein-LPS interaction during assembly.  Third,                  studies on the mechanism of export-coupled regulation by using                  signal sequence mutations and protein fusions in both OmpC and                  LamB to identify protein structural requirements to be either                   an initiator or a target of this regulatory control.                                                                                                            There is a growing appreciation in the field of protein export                  that the dog pancreas microsome-wheat germ extract system which                 yielded the discovery of SRP and docking protein and so much                    other information is in fact a very atypical system since it is                 primarily co-translational.  Export into mitochondria and out                   of both bacteria and yeast seems to be primarily post-                          translational, and evidence for a particle analogous to SRP is                  lacking.  Thus the SRP-mediated elongation arrest can not                       operate in these systems, and if there is regulation coupled to                 export it must operate in a different fashion.  This group                      seems to have a handle on an alternative regulatory system                      which, although specialized, may be a prototype for many other                  systems.  This project is an attempt to define some of the                      basic parameters of this regulatory system as well as to                        examine the later steps in E. coli outer membrane protein                       export pathway such folding and interaction with small ligands.
{'FirstName': 'Carl', 'LastName': 'Schnaitman', 'PI_MID_INIT': 'A', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Carl A Schnaitman', 'EmailAddress': None, 'NSF_ID': '000290357', 'StartDate': '02/15/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Virginia Main Campus', 'CityName': 'CHARLOTTESVILLE', 'ZipCode': '229034833', 'PhoneNumber': '4349244270', 'StreetAddress': '1001 EMMET ST N', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Virginia', 'StateCode': 'VA', 'CONGRESSDISTRICT': '05', 'CONGRESS_DISTRICT_ORG': 'VA05', 'ORG_UEI_NUM': 'JJG6HU8PA4S5', 'ORG_LGL_BUS_NAME': 'RECTOR & VISITORS OF THE UNIVERSITY OF VIRGINIA', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8820633.xml'}