Structure and function of small heat shock proteins from the magnetotactic bacterium Magnetospirillum magneticum AMB-1

Tetsuya Abe*, Shinpei Ito, Naoya Nishi, Yoshihiro Tsukada, Takuo Yasunaga, Atsushi Arakaki, Tadashi Matsunaga, Masafumi Yohda

*この研究の対応する著者

研究成果: Article査読

1 被引用数 (Scopus)

抄録

In this study, we expressed, purified and characterized small heat shock proteins (sHsp) from a magnetotactic bacterium, Magnetospirillum magneticm AMB-1, Hsp17.5, Hsp17.8 and Hsp18.3. They all showed molecular chaperone activity to protect citrate synthase from thermal aggregation at 45°C. The oligomeric states were examined by size exclusion chromatography and electron microscopy. Hsp17.8 exists as a spherical oligomer like other sHsps, and the oligomer reversibly dissociates to small conformers, probably dimers, at elevated temperatures. On the contrary, Hsp17.5 and Hsp18.3 take large filamentous conformations. A similar structure was observed in an sHsp of Sulfolobus tokodaii, StHsp19.7, but it did not exhibit molecular chaperone activity. Hsp17.5 and Hsp18.3 changed their oligomeric states according to the elevation of temperature. Among them, Hsp17.5 exhibited reversible dissociation. This is the first report that the filamentous sHsp exhibit molecular chaperone activity with the change of oligomeric states.

本文言語English
ページ(範囲)698-704
ページ数7
ジャーナルKobunshi Ronbunshu
67
12
DOI
出版ステータスPublished - 2010 12
外部発表はい

ASJC Scopus subject areas

  • ポリマーおよびプラスチック
  • 環境科学(全般)
  • 材料科学(その他)
  • 化学工学(その他)

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