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THE PLANT CELL, Vol 3, Issue 2 169-174, Copyright © 1991 by American Society of Plant Biologists


RESEARCH ARTICLES

Site-Specific Mutagenesis of the D1 Subunit of Photosystem II in Wild-Type Chlamydomonas

E. Przibilla, S. Heiss, U. Johanningmeier and A. Trebst
Ruhr-Universitat Bochum, Lehrstuhl fur Biochemie der Pflanzen, Postfach 102148, D-4630 Bochum, Federal Republic of Germany

The structure and functional mode of photosystem II reaction center protein D1 can be studied by analyzing the effects of amino acid substitutions within the binding niche for QB, the second stable electron acceptor of photosystem II, on herbicide binding. Here we report on site-directed mutagenesis of the psbA gene coding for the D1 protein in the unicellular alga Chlamydomonas reinhardtii. The chloroplasts of wild-type cells were transformed using the particle gun. The plasmids introduced carried an in vitro mutated fragment of the psbA gene. We obtained a double mutant with replacements of amino acids 264 and 266 and a triple mutant having an additional substitution in position 259. The sensitivities of both mutants toward several types of herbicides are given and compared with those of a mutant having only a substitution at position 264.


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J. Biol. Chem.Home page
A. Lardans, N. W. Gillham, and J. E. Boynton
Site-directed Mutations at Residue 251of the Photosystem II D1 Protein of Chlamydomonas That Result in a Nonphotosynthetic Phenotype and Impair D1 Synthesis and Accumulation
J. Biol. Chem., January 3, 1997; 272(1): 210 - 216.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
J. P. Whitelegge, D. Koo, B. A. Diner, I. Domian, and J. M. Erickson
Assembly of the Photosystem II Oxygen-evolving Complex Is Inhibited in psbA Site-directed Mutants of Chlamydomonas reinhardtii
J. Biol. Chem., January 6, 1995; 270(1): 225 - 235.
[Abstract] [Full Text] [PDF]




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Copyright © 1991 by the American Society of Plant Biologists