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

FEBS Letters

Guillain, Florent¹  Mintz, Elisabeth¹  Catty, Patrice¹  Bal, Nathalie¹ 

[1] Commissariat à l'Energie Atomique, Département de Biologie Moléculaire et Structurale, Laboratoire de Biophysique Moléculaire et Cellulaire, UMR CEA-CNRS-UJF 5090, 17 rue des Martyrs, 38054 Grenoble Cedex 09, France

关键词: Cadmium;    Metal-binding domain;    P-type ATPase;    CadA;   

DOI  :  10.1016/S0014-5793(01)02927-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using the baculovirus/Sf9 expression system, we produced CadA and ΔMBD, 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. ΔMBD 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.

【 授权许可】

Unknown