The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
CopA: An Escherichia coli Cu(I)-translocating P-type ATPase
Open accessAbstract
The copA gene product, a putative copper-translocating P-type ATPase, has been shown to be involved in copper resistance in Escherichia coli . The copA gene was disrupted by insertion of a kanamycin gene through homologous recombination. The mutant strain was more sensitive to copper salts but not to salts of other metals, suggesting a role in copper homeostasis. The copper-sensitive phenotype could be rescued by complementation by a plasmid carrying copA from E. coli or copB from Enterococcus hirae . Expression of copA was induced by salts of copper or silver but not zinc or cobalt. Everted membrane vesicles from cells expressing copA exhibited ATP-coupled accumulation of copper, presumably as Cu(I). The results indicate that CopA is a Cu(I)-translocating efflux pump that is similar to the copper pumps related to Menkes and Wilson diseases and provides a useful prokaryotic model for these human diseases.
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Cites
Measurement of protein using bicinchoninic acid
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482
The ZnuABC high‐affinity zinc uptake system and its regulator Zur in Escherichia coli
Patzer, S. I., & Hantke, K. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00883.x · Cited by 490
The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase
Rensing, C., Mitra, B., & Rosen, B. P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14326 · Cited by 419
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Cited by
Bacterial silver resistance: molecular biology and uses and misuses of silver compounds
Silver, S. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00047-0 · Cited by 1,312
The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
Macomber, L., & Imlay, J. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812808106 · Cited by 1,117
Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion Receptors
Finney, L. A., & O'Halloran, T. V. (2003) · Science · doi:10.1126/science.1085049 · Cited by 1,100
Function and Regulation of Human Copper-Transporting ATPases
Lutsenko, S., Barnes, N. L., Bartee, M. Y., & Dmitriev, O. Y. (2007) · Physiological Reviews · doi:10.1152/physrev.00004.2006 · Cited by 864
Molecular Analysis of the Copper-Transporting Efflux System CusCFBA of Escherichia coli
Franke, S., Grass, G., Rensing, C., & Nies, D. H. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.13.3804-3812.2003 · Cited by 538
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Metadata
- Authors
- Rensing, C., Fan, B., Sharma, R., Mitra, B., & Rosen, B. P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-01-18
- Volume
- 97
- Issue
- 2
- Pages
- 652-656
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1974939001
- Cited by
- 516
- References
- 3
- FWCI
- 21.22
- Type
- journal article
- Language
- en
- Open access
- bronze
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