Biochemical and Molecular Genetic Regulation of Sucrose     Phosphate Synthase in Leaves
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'M.  Paige', 'PO_EMAI': None, 'PO_PHON': None}
Sucrose phosphate synthase (SPS) is a key enzyme in                             determining the biochemical capacity of leaves for sucrose                      synthesis.  However, detailed knowledge of SPS at the                           biochemical and molecular genetic levels is lacking and must                    be obtained in order to understand the regulation of this                       pivotal enzyme.  Study at the molecular level can be stated                     as a result of obtaining monoclonal antibodies against the                      spinach leaf enzyme (polyclonals are in preparation).  Using                    the antibodies, direct evidence has been obtained for                           phosphorylation of SPS in vivo, and also a partial amino acid                   sequence has been determined from which and oligonucleotide                     probe will be made and used to isolate a cDNA.  The proposed                    studies will expand on these developments and examine the two                   subtypes of coarse control which regulate SPS activity in                       vivo: covalent modification mechanism; and 3) produce a DNA                     probe to the enzyme with which to begin studies of                              transcriptional/translational mechanisms that regulate the                      expression of the SPS gene.                                                                                                                                     This project investigates the enzymes which determines how                      much sucrose is made in leaves of plants, and thereby how                       much plant growth is possible.  This has been a very elusive                    enzyme but recent success in raising a monoclonal antibody                      now opens the door to a through study now opens the door to a                   through study of this critically important enzyme.***//
{'FirstName': 'Steven', 'LastName': 'Huber', 'PI_MID_INIT': 'C', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Steven C Huber', 'EmailAddress': 'schuber1@life.uiuc.edu', 'NSF_ID': '000341598', 'StartDate': '03/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'North Carolina State University', 'CityName': 'RALEIGH', 'ZipCode': '276950001', 'PhoneNumber': '9195152444', 'StreetAddress': '2601 WOLF VILLAGE WAY', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'North Carolina', 'StateCode': 'NC', 'CONGRESSDISTRICT': '02', 'CONGRESS_DISTRICT_ORG': 'NC02', 'ORG_UEI_NUM': 'U3NVH931QJJ3', 'ORG_LGL_BUS_NAME': 'NORTH CAROLINA STATE UNIVERSITY', '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': '8817414.xml'}