This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Silver, S Articles by Rosenberg, H Search for Related Content PubMed PubMed Citation Articles by Silver, S Articles by Rosenberg, H

 Previous Article  |  Next Article 

J Bacteriol. 1981 June; 146(3): 983-996

Inducible plasmid-determined resistance to arsenate, arsenite, and antimony (III) in escherichia coli and Staphylococcus aureus.

ABSTRACT

Plasmids in both Escherichia coli and Staphylococcus aureus contain an "operon" that confers resistance to arsenate, arsenite, and antimony(III) salts. The systems were always inducible. All three salts, arsenate, arsenite, and antimony(III), were inducers. Mutants and a cloned deoxyribonucleic acid fragment from plasmid pI258 in S. aureus have lost arsenate resistance but retained resistances to arsenite and antimony, demonstrating that separate genes are involved. Arsenate-resistant arsenite-sensitive S. aureus plasmid mutants were also isolated. In E. coli, plasmid-determined arsenate resistance and reduced uptake were additive to that found with chromosomal arsenate resistance mutants. Arsenate resistance was due to reduced uptake of arsenate by the induced plasmid-containing cells. Under conditions of high arsenate, when some uptake could be demonstrated with the induced resistant cells, the arsenate was rapidly lost by the cells in the absence of extracellular phosphate. Sensitive cells retained arsenate under these conditions. When phosphate was added, phosphate-arsenate exchange occurred. High phosphate in the growth medium protected cells from arsenate, but not from arsenite or antimony(III) toxicity. We do not know the mechanisms of arsenite or antimony resistance. However, arsenite was not oxidized to less toxic arsenate. Since cell-free medium "conditioned" by prior growth to induced resistant cells with toxic levels of arsenite or antimony(III) retained the ability to inhibit the growth of sensitive cells, the mechanism of arsenite and antimony resistance does not involve conversion of AsO2- or SbO+ to less toxic forms or binding by soluble thiols excreted by resistant cells.

This article has been cited by other articles:

• Saltikov, C. W., Olson, B. H. (2002). Homology of Escherichia coli R773 arsA, arsB, and arsC Genes in Arsenic-Resistant Bacteria Isolated from Raw Sewage and Arsenic-Enriched Creek Waters. Appl. Environ. Microbiol. 68: 280-288 [Abstract] [Full Text]  
• Romach, E. H., Zhao, C. Q., Razo, L. M. D., Cebrian, M. E., Waalkes, M. P. (2000). Studies on the Mechanisms of Arsenic-Induced Self Tolerance Developed in Liver Epithelial Cells through Continuous Low-Level Arsenite Exposure. Toxicol Sci 54: 500-508 [Abstract] [Full Text]  
• Rensing, C., Ghosh, M., Rosen, B. P. (1999). Families of Soft-Metal-Ion-Transporting ATPases. J. Bacteriol. 181: 5891-5897 [Full Text]  
• Sato, T., Kobayashi, Y. (1998). The ars Operon in the skin Element of Bacillus subtilis Confers Resistance to Arsenate and Arsenite. J. Bacteriol. 180: 1655-1661 [Abstract] [Full Text]  
• Suzuki, K., Wakao, N., Kimura, T., Sakka, K., Ohmiya, K. (1998). Expression and Regulation of the Arsenic Resistance Operon of Acidiphilium multivorum AIU 301 Plasmid pKW301 in Escherichia coli. Appl. Environ. Microbiol. 64: 411-418 [Abstract] [Full Text]  
• Li, J., Liu, S., Rosen, B. P. (1996). Interaction of ATP Binding Sites in the ArsA ATPase, the Catalytic Subunit of the Ars Pump. J. Biol. Chem. 271: 25247-25252 [Abstract] [Full Text]  
• Xu, C., Shi, W., Rosen, B. P. (1996). The Chromosomal arsR Gene of Escherichia coli Encodes a trans-acting Metalloregulatory Protein. J. Biol. Chem. 271: 2427-2432 [Abstract] [Full Text]