Competitive inhibition analysis of the enzyme-substrate interaction in the carboxy-terminal processing of the precursor D1 protein of photosystem II reaction center using substituted oligopeptides

Yumiko Yamamoto, Kimiyuki Satoh

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Abstract: A clear parallelism was demonstrated between the efficiency as substrate of the substituted oligopeptides corresponding to the carboxy- terminal (C-terminal) sequence of the precursor D1 protein (pD1) in the in vitro enzymatic assay and their competitive inhibitory capacity toward the proteolytic C-terminal processing of the full-length pD1 integrated in the intact photosystem II complex embedded in the thylakoid membrane of Scenedesmus obliguus LF-1 mutant, as shown e.g. by the influence of L343A, A345G and A345V substitutions and the effect of C-terminal fragments. This suggests that the basic mechanism for substrate recognition by the processing protease elucidated in the enzymatic analysis using synthetic oligopeptides is also effective in vivo, although it can sometimes be difficult to detect the consequence of amino acid substitution in the integrated systems.

Original languageEnglish
Pages (from-to)261-265
Number of pages5
JournalFEBS Letters
Volume430
Issue number3
DOIs
Publication statusPublished - Jul 3 1998

Keywords

  • C-terminal processing
  • Competitive inhibition
  • D1 protein
  • Photosystem II
  • Processing protease
  • Synthetic oligopeptide

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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