A possible regulatory role for the metal-binding domain of CadA, the Listeria monocytogenes Cd2+-ATPase

被引：34

作者：

Bal, N ^{[1
]}

Mintz, E ^{[1
]}

Guillain, F ^{[1
]}

Catty, P ^{[1
]}

机构：

[1] UFJ, CNRS, CEA,Dept BIol Mol & Struct, UMR 5090,Lab Biophys Mol & Cellulaire, F-38054 Grenoble 09, France

来源：

FEBS LETTERS | 2001年 / 506卷 / 03期

关键词：

cadmium; metal-binding domain; P-type ATPase; CadA;

D O I：

10.1016/S0014-5793(01)02927-1

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：

Using the baculovirus/Sf9 expression system, we produced CadA and Delta MBD, a metal-binding domain, truncated CadA. Both proteins had the expected properties of P-type ATPases: ATP-induced Cd2+ accumulation, Cd2+-sensitive ATP and Pi phosphorylation and ATPase activity. Delta MBD displayed lower initial transport velocity as well as lower maximal ATPase activity than CadA. MBD truncation flattened the Cd2+ dependence of the ATPase activity and increased apparent Cd2+ affinity, suggesting a positive cooperativity between MBD and membranous transport sites. We propose that occupancy of MBD by Cd2+ modulates CadA activity. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：249 / 252

页数：4

共 26 条

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