The presequence of the precursor to the nucleus-encoded 30 kDa protein of photosystem II in Euglena gracilis Z includes two hydrophobic domains

Yasushi Shigemori, Junko Inagaki, Hitoshi Mori, Mikio Nishimura, Sumio Takahashi, Yasusi Yamamoto

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

A cDNA clone for the extrinsic 30 kDa protein (OEC30) of photosystem II in Euglena gracilis Z was isolated and characterized. The open reading frame of the cDNA encoded a polypeptide of 338 amino acids, which consisted of a long presequence of 93 amino acids and a mature polypeptide of 245 amino acids. Two hydrophobic domains were identified in the presequence, in contrast to the presence of a single hydrophobic domain in the presequence of the corresponding proteins from higher plants. At the N- and C-terminal regions, respectively, of the presequence, a signal-peptide-like sequence and a thylakoid-transfer domain were identified. The presence of a long and unique presequence in the precursor to OEC30 is probably related to the complexity of the intracellular processes required for the synthesis and/or transport of the protein in Euglena.

Original languageEnglish
Pages (from-to)209-215
Number of pages7
JournalPlant Molecular Biology
Volume24
Issue number1
DOIs
Publication statusPublished - Jan 1 1994

Keywords

  • Euglena gracilis Z
  • cDNA cloning
  • chloroplast
  • oxygen-evolving complex
  • protein transport

ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Genetics
  • Plant Science

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