Regulatory Role of Plant Protein Kinases
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Parag R. Chitnis', 'PO_EMAI': None, 'PO_PHON': None}
By probing plant cDNA libraries sequentially with two partially                 degenerate oligonucleotides corresponding to highly conserved                   domains of mammalian serine protein kinases, a clone (PVPK-1)                   that encodes a putative plant protein kinase has recently been                  identifed.  This clone has striking homology to mammalian cAMP-                 dependent protein kinases.  This development now provides the                   basis for examination of the structure, organization and                        regulation of plant protein kinase gene families and dissection                 of the function of individual protein kinases in specific signal                transduction pathways that regulate development, mediate                        environmental responses and integrate metabolism.                                                                                                               Specific objectives are: (a) use of these and existing cloned                   sequences to determine the organization of families and sub-                    families of protein kinase genes; (b) isolation, characterization               and nucleotide sequence analysis of genomic sequences                           corresponding to cloned PVPK-1 cDNA; (c) generation of specific                 antibodies against PVPK-1 protein kinase; (d) immunoaffinity                    purification of the biochemical properties of PVPK-1 protein                    kinase; and (e) analysis of function by expression of wild-type                 and mutant PVPK-1 genes in protoplasts and in stable transgenic                 plants.                                                                                                                                                         Relatively little is known at the molecular level about signal                  transduction and response-coupling mechanisms that control plant                growth and development.  Protein kinase-mediated phosphorylation                of specific proteins is a major strategy for regulation of                      protein and enzyme activity in the transduction of environmental,               developmental and metabolic signals in animals and simple                       eukaryotes.  In higher plants, while protein phosphorylation has                been observed in vivo and protein kinase activity in vitro,                     little information is available on the molecular properties of                  plant protein kinases, their number and diversity with respect to               regulatory inputs and protein substrate outputs, or the function                of protein kinases in specific signal transduction pathways.                    This research begins to fill this information gap.
{'FirstName': 'Michael', 'LastName': 'Lawton', 'PI_MID_INIT': 'A', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Michael A Lawton', 'EmailAddress': 'lawton@aesop.rutgers.edu', 'NSF_ID': '000400324', 'StartDate': '10/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'The Salk Institute for Biological Studies', 'CityName': 'LA JOLLA', 'ZipCode': '920371002', 'PhoneNumber': '8584534100', 'StreetAddress': '10010 N TORREY PINES RD', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '50', 'CONGRESS_DISTRICT_ORG': 'CA50', 'ORG_UEI_NUM': 'NNJ6BMBTFGN5', 'ORG_LGL_BUS_NAME': 'SALK INSTITUTE FOR BIOLOGICAL STUDIES, SAN DIEGO, CALIFORNIA, THE', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '114400', 'Text': 'Molecular Biophysics'}, {'Code': '914500', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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