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

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

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)6863-6866
Number of pages4
JournalBiochemistry
Volume54
Issue number46
DOIs
Publication statusPublished - Nov 6 2015
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry

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