Structure and Function of Fission Yeast Signal Recognition  Particle
{'Code': '08070600', '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}
Signal recognition particle (SRP), a ribonucleoprotein composed of          six protein subunits and one molecule of 7SL RNA, is the first element          of the specialized machinery which recognizes proteins destined for             export from eukaryotic cells via the secretory pathway.  Based on in            vitro experiments, it has been postulated that, upon emergence of the           signal sequence from the ribosome, SRP binds and arrests translation.           When the complex arrives at the endoplasmic reticulum (ER) membrane, SRP        interacts with a specific receptor, dissociates, and translation of the         protein resumes accompanied by vectorial translocation into the ER              lumen.  By exploiting the unique advantages of the fission yeast                Schizosaccharomyces pombe, we will genetically and biochemically dissect        secretory protein targeting, focusing first on the essential 7SL                component of SRP.  Random mutagenesis of the cloned gene followed by            transformation and screening for conditional or partial secretory               defects will identify nucleotides which are critical for function in            vivo.  Conserved sequences and structures will be determined by                 comparison of 7SL homologs from divergent organisms, allowing generation        of specific models for its mode of action which will be tested by site-         directed mutagenesis of the S. pombe gene.  Suppressor selection will           identify other components which interact with 7SL RNA, minimally the            fission yeast SRP proteins; other likely targets include the SRP                receptor and ribosomal proteins.  Concurrent with the genetic                   experiments, a homologous in vitro system will be developed to study SRP        function; it will also be useful for biochemically characterizing               defects in the mutants.  These studies will provide insight into the            mechanism by which cell sort proteins, the salient features of which are        conserved between fission yeast and humans.
{'FirstName': 'Jo Ann', 'LastName': 'Wise', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Jo Ann Wise', 'EmailAddress': 'jaw17@case.edu', 'PI_PHON': '2163681876', 'NSF_ID': '000273811', 'StartDate': '08/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Illinois at Urbana-Champaign', 'CityName': 'URBANA', 'ZipCode': '618013620', 'PhoneNumber': '2173332187', 'StreetAddress': '506 S WRIGHT ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Illinois', 'StateCode': 'IL', 'CONGRESSDISTRICT': '13', 'CONGRESS_DISTRICT_ORG': 'IL13', 'ORG_UEI_NUM': 'Y8CWNJRCNN91', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF ILLINOIS', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1114', 'Text': 'Cellular Dynamics and Function'}, {'Code': '1132', 'Text': 'CELLULAR ORGANIZATION'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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