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Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae

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Odermatt, A., Suter, H., Krapf, R., Solioz, M.·1993·Journal of Biological Chemistry

Abstract

We cloned an operon, copAB, from Enterococcus hirae encoding two P-type ATPases of 727 and 745 amino acids, respectively. Both enzymes display heavy metal ion binding motifs in their polar N-terminal region. With an antibody against CopB, we showed on Western blots that expression of the operon is induced by either low or high ambient copper concentrations. Disruption of the copA gene renders the cells dependent, whereas copper disruption of copB results in a copper-sensitive phenotype. CopA exhibits 35% sequence similarity to CopB and 43% similarity to the ATPase encoded by the recently cloned human Mc1 gene, a gene responsible for the Menkes inborn error of copper metabolism. Our results imply that CopA and CopB are heavy metal ion ATPases that regulate the cytoplasmic copper activity, with CopA serving in the uptake and CopB in the extrusion of copper.

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Metadata

Authors
Odermatt, A., Suter, H., Krapf, R., & Solioz, M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1993-06
Volume
268
Issue
17
Pages
12775-12779
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2076000335
Cited by
377
References
0
FWCI
27.05
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. https://app.cochat.ai/papers/10.1016/s0021-9258(18)31455-8
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Odermatt, A., Suter, H., Krapf, R., & Solioz, M. (1993). Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)31455-8

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