A sequential two-step proteolytic process in the carboxyl-terminal truncation of precursor D1 protein in Synechocystis sp. PCC6803

Noritoshi Inagaki, Yumiko Yamamoto, Kimiyuki Satoh

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

The D1 protein of photosystem II is synthesized in precursor with a carboxyl-terminal extension. Interestingly, there is quite a range in chain length of the extension, which roughly depends upon the class of organisms. In cyanobacteria, e.g. in Synechocystis sp. PCC6803, the extension consists of 16 amino acid residues, seven residues longer than its counterpart in higher plants. In this study, we examined the D1 processing in Synechocystis sp. PCC6803 by pulse-chase experiments and detected a proteolytic intermediate of this process. This finding suggests that the elongated extension in this organism is excised with a sequential two-step proteolysis, which differs markedly from the manner observed in higher plants.

Original languageEnglish
Pages (from-to)197-201
Number of pages5
JournalFEBS Letters
Volume509
Issue number2
DOIs
Publication statusPublished - Dec 7 2001

Fingerprint

Proteolysis
Synechocystis
Photosystem II Protein Complex
Protein Precursors
Chain length
Amino Acids
Cyanobacteria
Processing
Proteins
Experiments

Keywords

  • Carboxyl-terminal processing protease
  • D1 protein
  • Photosystem II
  • Synechocystis sp. PCC6803

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A sequential two-step proteolytic process in the carboxyl-terminal truncation of precursor D1 protein in Synechocystis sp. PCC6803. / Inagaki, Noritoshi; Yamamoto, Yumiko; Satoh, Kimiyuki.

In: FEBS Letters, Vol. 509, No. 2, 07.12.2001, p. 197-201.

Research output: Contribution to journalArticle

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