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

Fumiko Taguchi, Yuichiro Takahashi, Kimiyuki Satoh

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4 Citations (Scopus)

Abstract

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 carboxylterminal processing of the D1 precursor in the photosystem II reaction center is a rate-limiting step for growth under some environmental stress conditions.

Original languageEnglish
Pages (from-to)1324-1329
Number of pages6
JournalPlant and Cell Physiology
Volume39
Issue number12
Publication statusPublished - Dec 1998

Fingerprint

Chlamydomonas
D1 protein
Protein Precursors
mixed culture
amino acid substitution
Amino Acid Substitution
viability
mutants
Growth
Light
Chlamydomonas reinhardtii
oligopeptides
Oligopeptides
Photosystem II Protein Complex
Darkness
photosystem II
light intensity
proteins

Keywords

  • C-terminal processing
  • Chlamydomonas reinhardtii
  • D1 protein
  • Mixed-culture
  • Viability

ASJC Scopus subject areas

  • Plant Science
  • Physiology
  • Cell Biology

Cite this

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abstract = "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 carboxylterminal processing of the D1 precursor in the photosystem II reaction center is a rate-limiting step for growth under some environmental stress conditions.",
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T1 - Viability of chlamydomonas mutants with amino acid substitutions in the precursor D1 protein at the carboxyl-terminal processing site

T2 - An analysis by mixed-culture growth experiments

AU - Taguchi, Fumiko

AU - Takahashi, Yuichiro

AU - Satoh, Kimiyuki

PY - 1998/12

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N2 - 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 carboxylterminal processing of the D1 precursor in the photosystem II reaction center is a rate-limiting step for growth under some environmental stress conditions.

AB - 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 carboxylterminal processing of the D1 precursor in the photosystem II reaction center is a rate-limiting step for growth under some environmental stress conditions.

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