Effect of phenol-induced changes in lipid composition on conformation of OmpF-like porin of Yersinia pseudotuberculosis

被引:13
|
作者
Sanina, Nina [1 ]
Davydova, Ludmila [1 ]
Bakholdina, Svetlana [2 ]
Novikova, Olga [2 ]
Pornyagina, Olga [1 ,2 ]
Solov'eva, Tamara [2 ]
Shnyrov, Valery [3 ]
Bogdanov, Mikhail [4 ]
机构
[1] Far Eastern Fed Univ, Dept Biochem Microbiol & Biotechnol, Vladivostok 690600, Russia
[2] Russian Acad Sci, Pacific Inst Bioorgan Chem, Vladivostok 690022, Russia
[3] Univ Salamanca, Dept Biochem & Mol Biol, E-37008 Salamanca, Spain
[4] Univ Texas Houston, Sch Med, Dept Biochem & Mol Biol, Houston, TX USA
关键词
Lipid; Lysophosphatidylethanolamine; Porin; Protein conformation; DSC; Intrinsic protein fluorescence; OUTER-MEMBRANE PROTEIN; FORMING PROTEIN; PHASE; LYSOPHOSPHOLIPIDS; BACTERIA; BILAYERS;
D O I
10.1016/j.febslet.2013.05.056
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The present work aimed to compare the effects of different lysophosphatidylethanolamine (LPE) content in lipids derived from Yersinia pseudotuberculosis cells exposed and not exposed to phenol on the conformation of OmpF-like porin of these bacteria. Differential scanning calorimetry and intrinsic protein fluorescence showed that the 2.5-fold increase of LPE content and the corresponding increase in the phase transition temperature of bacterial lipids were accompanied by enhanced protein thermostability. Integral conformational rearrangement of protein was supported by drastic changes in the microenvironment of the tryptophan residues, likely resulting in a convergence of monomers in trimeric porin and exposure of outer tryptophan residues to the water environment. These conformational changes may impede the porin channel permeability under stress conditions in bacteria. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2260 / 2265
页数:6
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