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PMID: 8037745 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Induction of the putative copper ATPases, CopA and CopB, of Enterococcus hirae by Ag+ and Cu2+, and Ag+ extrusion by CopB.

Biochemical and biophysical research communications ·Vol. 202 ·No. 1 ·1994-07-15 ·Pages 44-8

Odermatt A, Krapf R, Solioz M

Abstract

The two P-type ATPases CopA and CopB are effecting regulation of cellular copper activity in Enterococcus hirae. With antibodies against these ATPases, we showed on Western blots the simultaneous induction of CopA and CopB by copper or silver ions. Copper contents of wild type and mutant cells lacking either CopA, CopB or both enzymes were measured by atomic absorption. Strains disrupted in copB showed clearly enhanced copper contents. Mutants lacking CopB also lost the ability of energy dependent efflux of silver ions. Our results demonstrate that CopA and CopB are under the same genetic control and support the proposal that CopB is a copper and silver exporting ATPase.

Related Genes
MeSH Terms
Adenosine Triphosphatases/biosynthesis Bacterial Outer Membrane Proteins Bacterial Proteins/biosynthesis Carrier Proteins/biosynthesis Cation Transport Proteins Copper/metabolism,pharmacology Copper Transport Proteins Copper-Transporting ATPases Enterococcus/drug effects,enzymology,genetics Enzyme Induction Kinetics Operon Silver/pharmacology
Chemicals
Bacterial Outer Membrane Proteins Bacterial Proteins Carrier Proteins Cation Transport Proteins CopA protein, Bacteria Copper Transport Proteins Silver Copper Adenosine Triphosphatases CopB ATPase, Enterococcus hirae Copper-Transporting ATPases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Odermatt A
Department of Clinical Pharmacology, University of Berne, Switzerland.
Krapf R
Solioz M
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1994-07-15
Pages
44-8
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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