Partial degradation of the 18-kDa protein of the photosynthetic oxygen-evolving complex: A study of a binding site

Tomohiko Kuwabara, Teruyo Murata, Mitsue Miyao, Norio Murata

研究成果: Article査読

65 被引用数 (Scopus)

抄録

When the NaCl extract from spinach Photosystem II particles was dialyzed against a low-salt medium, the 18-kDa protein slowly degraded to a fragment of 17 kDa. This observation suggests that a proteinase previously associated with the Photosystem II particles in a latent form was activated by dissociation with NaCl. The 18-kDa protein and the 17-kDa fragment were purified, and their N-terminal amino acid sequences and total amino acid compositions were determined. These results determined 44 amino acid residues at the N-terminal of the 18-kDa protein, and suggest that 12 amino acid residues (mostly hydrophobic) at the N-terminal were lost by the degradation. The 18-kDa protein could rebind to the NaCl-treated and 24-kDa protein-supplemented Photosystem II particles and sustain their oxygen-evolution activity in a low-Cl- medium, whereas the 17-kDa fragment had lost these abilities. These observations suggest that the N-terminal region of the 18-kDa protein forms a domain which binds to Photosystem II particles.

本文言語English
ページ(範囲)146-155
ページ数10
ジャーナルBBA - Bioenergetics
850
1
DOI
出版ステータスPublished - 1986 6月 10
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 細胞生物学

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