A single amino acid residue is responsible for species-specific incompatibility between CCT and α-actin

被引：14

作者：

Altschuler, G. M. ^{[1
,3
]}

Dekker, C. ^{[1
]}

McCormack, E. A. ^{[1
]}

Morris, E. P. ^{[2
]}

Klug, D. R. ^{[3
]}

Willison, K. R. ^{[1
]}

机构：

[1] Inst Canc Res, Sect Cell & Mol Biol, London SW3 6JB, England

[2] Inst Canc Res, Sect Struct Biol, London SW3 6JB, England

[3] Univ London Imperial Coll Sci Technol & Med, Dept Chem, London SW7 2AZ, England

来源：

FEBS LETTERS | 2009年 / 583卷 / 04期

关键词：

Actin; ACT1; Muscle; CCT; Chaperonin; Protein folding; CYTOSOLIC CHAPERONIN; BINDING-SITES; BETA-ACTIN; MUSCLE; EVOLUTION; INTERACTS; SUBUNITS; INSIGHTS; COMPLEX;

D O I：

10.1016/j.febslet.2009.01.031

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：

Actin is dependent on the type-II chaperonin CCT (chaperonin containing TCP-1) to reach its native state. In vitro, yeast CCT folds yeast and also mammalian cytoplasmic (beta/gamma) actins but is now found to be incapable of folding mammalian skeletal muscle alpha-actin. Arrest of alpha-actin on yeast CCT at a folding cycle intermediate has been observed by electron microscopy. This discovery explains previous observations in vivo that yeast mutants expressing only the muscle actin gene are non-viable. Mutational analysis identified a single specific alpha-actin residue, Asn-297, that confers this species/isoform folding specificity. The implications of this incompatibility for chaperonin mechanism and actin CCT co-evolution are discussed. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：782 / 786

页数：5

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