Chloroplast Thylakoid Protein Phosphatase
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Kamal Shukla', 'PO_EMAI': None, 'PO_PHON': None}
Chloroplast Thylakoid Protein Phosphatase:  This project                   will continue the characterization of two protein phosphatases                  associated with chloroplast thylakoid membranes isolated from                   wheat (Triticum aestivum).  Characterization will include                       kinetic analysis of the activities, studies on substrate                        specificity using endogenous and synthetic peptides, and                        biochemical analysis of tertiary and quaternary structures.                     Antibodies recognizing the phosphatases will be prepared and                    used in studies on the location of the phosphatase enzymes                      within the photosynthetic membrane network.  If antibodies                      inhibit the enzymatic activity, they will be utilized to                        substantiate that phosphatase activity is involved in the                       reversal of State 1/State 2 transition, which regulates                         photosynthetic energy production.  Antibodies will also be used                 to study the amphiphilic properties of the enzyme, i.e., the                    potential to partition between the thylakoid surface and stromal                phase, and the potential of this process to regulate protein                    dephosphorylation, thereby complementing known mechanisms of                    modulating thylakoid protein kinase activity.                                                                                                                   Chloroplast thylakoid membrane protein phosphorylation plays an                 important role in the regulation of steady-state energy                         production by photosynthesis.  The key elements are a protein                   kinase whose activity is stimulated when the plastoquinone pool                 is reduced, and the light-harvesting complex, thereby                           differentially partitions between the two photosystems.  This                   system is thought to govern the photon flux density between the                 two photosystems.  The protein kinases present in the thylakoid                 membrane have been characterized, but the protein phosphatases,                 which reverse the light-harvesting complex phosphorylation, are                 little understood.  The results are essential to a complete                     understanding of how photosynthetic organisms are able to                       optimize their efficiency.  Such information may also be useful                 to engineering or breeding desirable molecular response traits                  into commercially useful plants.
{'FirstName': 'John', 'LastName': 'Markwell', 'PI_MID_INIT': 'P', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'John P Markwell', 'EmailAddress': 'markwell@unl.edu', 'NSF_ID': '000309655', 'StartDate': '09/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Nebraska-Lincoln', 'CityName': 'LINCOLN', 'ZipCode': '685032427', 'PhoneNumber': '4024723171', 'StreetAddress': '2200 VINE ST # 830861', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Nebraska', 'StateCode': 'NE', 'CONGRESSDISTRICT': '01', 'CONGRESS_DISTRICT_ORG': 'NE01', 'ORG_UEI_NUM': 'HTQ6K6NJFHA6', 'ORG_LGL_BUS_NAME': 'BOARD OF REGENTS OF THE UNIVERSITY OF NEBRASKA', 'ORG_PRNT_UEI_NUM': None}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '114400', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8703100.xml'}