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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

Viability of Chlamydomonas Mutants with Amino Acid Substitutions in the Precursor D1 Protein at... Abstract 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. © 1998. The Japanese Society of Plant Physiologists (JSPP) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant and Cell Physiology Oxford University Press

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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Publisher
Oxford University Press
Copyright
© 1998. The Japanese Society of Plant Physiologists (JSPP)
ISSN
0032-0781
eISSN
1471-9053
DOI
10.1093/oxfordjournals.pcp.a029337
Publisher site
See Article on Publisher Site

Abstract

Abstract 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. © 1998. The Japanese Society of Plant Physiologists (JSPP)

Journal

Plant and Cell Physiology – Oxford University Press

Published: Dec 1, 1998

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