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

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Tanaka K,Caaveiro JM,Tsumoto K

doi

10.1021/acs.biochem.5b01112

subject

Has Abstract

pub_date

2015-11-24 00:00:00

pages

6863-6

issue

46

eissn

0006-2960

issn

1520-4995

journal_volume

54

pub_type

杂志文章