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

    Research output: Contribution to journalArticlepeer-review

    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
    DOIs
    Publication statusPublished - Dec 1998

    Keywords

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

    ASJC Scopus subject areas

    • Physiology
    • Plant Science
    • Cell Biology

    Fingerprint

    Dive into the research topics of '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'. Together they form a unique fingerprint.

    Cite this