Biochemical characterization of a novel ArsA ATPase complex from Alkaliphilus metalliredigens QYMF

被引：13

作者：

Fu, Hsueh-Liang ^{[2
]}

Rosen, Barry P. ^{[1
]}

Bhattacharjee, Hiranmoy ^{[1
]}

机构：

[1] Florida Int Univ, Dept Cellular Biol & Pharmacol, Herbert Wertheim Coll Med, Miami, FL 33199 USA

[2] Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, Detroit, MI 48201 USA

来源：

FEBS LETTERS | 2010年 / 584卷 / 14期

基金：

美国国家卫生研究院;

关键词：

ArsA; Arsenite; Antimonite; Acr3; ArsB; Detoxification; ANION-TRANSLOCATING ATPASE; NUCLEOTIDE-BINDING SITE; ESCHERICHIA-COLI; SACCHAROMYCES-CEREVISIAE; ARSENIC DETOXIFICATION; CATALYTIC SUBUNIT; PROTEIN; PUMP; GENE; MUTAGENESIS;

D O I：

10.1016/j.febslet.2010.05.044

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 two putative ars operons in Alkaliphilus metalliredigens QYMF are distinctive in that the arsA gene is split in halves, amarsA1 and amarsA2, and, acr3 but not an arsB gene coexists with arsA. Heterologous expression of one of the A. metalliredigens ars operons (ars1) conferred arsenite but not antimonite resistance to Delta ars Escherichia coli. Only the co-expressed AmArsA1 and AmArsA2 displayed arsenite or antimonite stimulated ATPase activity. The results show that AmArsA1-AmArsA2 interaction is needed to form the functional ArsA ATPase. This novel AmArsA1-AmArsA2 complex may provide insight in how it participates with Acr3 in arsenite detoxification. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3089 / 3094

页数：6

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