Bidirectional Transformation of a Metamorphic Protein between the Water-Soluble and Transmembrane Native States

Koji Tanaka, Jose M.M. Caaveiro, Kouhei Tsumoto

研究成果: Contribution to journalArticle査読

13 被引用数 (Scopus)

抄録

The bidirectional transformation of a protein between its native water-soluble and integral transmembrane conformations is demonstrated for FraC, a hemolytic protein of the family of pore-forming toxins. In the presence of biological membranes, the water-soluble conformation of FraC undergoes a remarkable structural reorganization generating cytolytic transmembrane nanopores conducive to cell death. So far, the reverse transformation from the native transmembrane conformation to the native water-soluble conformation has not been reported. We describe the use of detergents with different physicochemical properties to achieve the spontaneous conversion of transmembrane pores of FraC back into the initial water-soluble state. Thermodynamic and kinetic stability data suggest that specific detergents cause an asymmetric change in the energy landscape of the protein, allowing the bidirectional transformation of a membrane protein.

本文言語英語
ページ(範囲)6863-6866
ページ数4
ジャーナルBiochemistry
54
46
DOI
出版ステータス出版済み - 11 6 2015
外部発表はい

All Science Journal Classification (ASJC) codes

  • Biochemistry

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