The Role of the D2 Protein in the Photosystem II Complex as Probed by Directed Mutagenesis and Mutant Analysis
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{'SignBlockName': 'Kamal Shukla', 'PO_EMAI': None, 'PO_PHON': None}
The D2 protein is a central component of the Photosystem II                     complex in photosynthetic membranes, but its precise function is                unknown.  The role of specific amino acid residues and                          polypeptide regions of D2 in function, structure and assembly of                the Photosystem II complex is being studied by directed                         mutagenesis techniques.  Specific mutations are induced D2.  The                psbD-I gene (encoding D2) carrying site-directed mutations is                   introduced into a mutant of the transformable photoheterotrophic                cyanobacterium Synechocystis 6803, from which the two psbD gene                 copies (psbD-I and psbD-II) have been deleted.  Target regions to               create D2 mutations are identified in part by comparison with the               partially homologous M subunit of the reaction center from purple               bacteria, for which the detailed structure is known.  The                       properties of the mutant Photosystem II complex are analyzed in a               variety of ways, including mRNA studies, and analysis of                        Photosystem II protein composition and synthesis, electron                      transport, chlorophyll fluorescence, specific EPR signals,                      herbicide binding, and flash-induced absorbance changes.                                                                                                        The results of this project will lead to a detailed understanding               of the role of specific residues and regions in an important but                poorly understood protein in photosynthetic membranes.  Insight                 will be gained on how the oxidizing complex is organized.                       Potentially significant is that the protein complex can be                      altered to result in more efficient operation.***//
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[{'Code': '1144', 'Text': 'Molecular Biophysics'}, {'Code': '9120', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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