Analysis of Functional Regions of a Chloroplast Transit     Peptide
{'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}
Previous work focussed on analysis of protein transport into                    chloroplasts using the small subunit of ribulose-1,5-bisphosphate               carboxylase, pSSU, as the model.  The effects of deletion mutations in          the pSSU transit peptide (TP) which is essential for protein import             were studied.  Based on those results, mutants will now be generated            with changes in the carboxyterminal and central regions of the TP.              Site-directed mutagenesis will be used to alter a small number of               specific residues previously identified as crucial to protein transport         in those regions.  Since functional residues in the aminoterminal               region are less well defined, mutants in this region will be created by         random chemical mutagenesis.  Mutants will be analyzed for membrane             binding, processing steps, and ATP requirements for transport.                  Preproteins, which are either located in the stroma or in the thylakoid         membrane, will be isolated.  They will be used to target and isolate            different membrane receptor classes.  Synthetic peptides representing           functional regions of TP will be used for the isolation of membrane             receptor components, which will be characterized.  The long-term goal           is to generate a mechanistic model of the transport process.                      The complexity of eucaryotic cells makes it necessary to target               proteins to specific compartments which separate metabolic pathways.            The routes to various major subcellular (and extracellular)                     compartments differ in specific ways.  Even among different types of            cells, the sorting may differ.  For example, while green plants sort            proteins destined for the two distinctly different double-membrane-             enclosed intracellular compartments, mitochondria and for chloroplasts,         precisely distinctly, yeast cells (which lack chloroplasts) will use            the "chloroplast import signal" to target proteins into mitochondria.           The mechanism(s) whereby information encoded in the amino acid sequence         of specific proteins is "translated" into specific translocation into           appropriate compartments is a fundamental problem in cell biology,              which is addressed directly in this proposal.
[{'FirstName': 'Catherine', 'LastName': 'Wasmann', 'PI_MID_INIT': 'C', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Catherine C Wasmann', 'EmailAddress': None, 'NSF_ID': '000434884', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Co-Principal Investigator'}, {'FirstName': 'Hans', 'LastName': 'Bohnert', 'PI_MID_INIT': 'J', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Hans J Bohnert', 'EmailAddress': 'bohnerth@life.uiuc.edu', 'NSF_ID': '000485018', 'StartDate': '09/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}]
{'Name': 'University of Arizona', 'CityName': 'TUCSON', 'ZipCode': '85721', 'PhoneNumber': '5206266000', 'StreetAddress': '845 N PARK AVE RM 538', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Arizona', 'StateCode': 'AZ', 'CONGRESSDISTRICT': '07', 'CONGRESS_DISTRICT_ORG': 'AZ07', 'ORG_UEI_NUM': 'ED44Y3W6P7B9', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF ARIZONA', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '111400', 'Text': 'Cellular Dynamics and Function'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8812191.xml'}