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| PRIMARY STRUCTURE OF 2 P-TYPE ATPASES INVOLVED IN COPPER HOMEOSTASIS IN ENTEROCOCCUS-HIRAE |
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| Author(s): ODERMATT A, SUTER H, KRAPF R, SOLIOZ M |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 268 Issue: 17 Pages: 12775-12779 Published: JUN 15 1993 |
| Times Cited: 254 References: 38 |
| 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV BERN, DEPT CLIN PHARMACOL, MURTENSTR 35, CH-3010 BERN, SWITZERLAND
2. CANTONAL HOSP ST GALLEN, CH-9007 ST GALLEN, SWITZERLAND |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: LG658 |
| ISSN: 0021-9258 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |