Journal Article

Viability of <i>Chlamydomonas</i> Mutants with Amino Acid Substitutions in the Precursor D1 Protein at the Carboxyl-Terminal Processing Site: an Analysis by Mixed-Culture Growth Experiments

Fumiko Taguchi, Yuichiro Takahashi and Kimiyuki Satoh

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 39, issue 12, pages 1324-1329
Published in print December 1998 | ISSN: 0032-0781
Published online December 1998 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029337
Viability of Chlamydomonas Mutants with Amino Acid Substitutions in the Precursor D1 Protein at the Carboxyl-Terminal Processing Site: an Analysis by Mixed-Culture Growth Experiments

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Department of Biology, Faculty of Science, Okayama University, 3-1-1, Tsushima-naka, Okayama, 700-8530 Japan In order to analyze the influence of amino acid substitutions at the carboxyl-terminal processing site of the D1 precursor protein, mixed-culture growth experiments were conducted for psbA directed mutants of Chlamydomonas reinhardtii. Wild type and D1 mutants were mixed in the same culture and their viability was compared. Replacement of Ser-345 by Gly or Val at the cleavage site markedly affected the relative growth rate of the mutant in the high intensity light, but not in a dim light or the darkness. This was consistent with the previous result obtained by in vitro analysis using substituted carboxyl-terminal oligopeptides as substrates [Taguchi et al. (1995) J Biol. Chem. 270: 10711], This is a clear indication that the rate of carboxyl-terminal processing of the D1 precursor in the photosystem II reaction center is a rate-limiting step for growth under some environmental stress conditions.

Keywords: C-terminal processing; Chlamydomonas reinhardtii; D1 protein; Mixed-culture; Viability

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Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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