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 Harwood-Sears, V Articles by Gordon, A S Search for Related Content PubMed PubMed Citation Articles by Harwood-Sears, V Articles by Gordon, A S Agricola Articles by Harwood-Sears, V Articles by Gordon, A S

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1990 May; 56(5): 1327-1332

Copper-induced production of copper-binding supernatant proteins by the marine bacterium Vibrio alginolyticus.

Department of Biological Sciences, Old Dominion University, Norfolk, Virginia 23529.

ABSTRACT

Growth of the marine bacterium Vibrio alginolyticus is temporarily inhibited by micromolar levels of copper. During the copper-induced lag phase, supernatant compounds which complex and detoxify copper are produced. In this study two copper-inducible supernatant proteins having molecular masses of ca. 21 and 19 kilodaltons (CuBP1 and CuBP2) were identified; these proteins were, respectively, 25 and 46 times amplified in supernatants of copper-challenged cultures compared with controls. Experiments in which chloramphenicol was added to cultures indicated that there was de novo synthesis of these proteins in response to copper. When supernatants were separated by gel permeation chromatography, CuBP1 and CuBP2 coeluted with a copper-induced peak in copper-binding activity. CuBP1 and CuBP2 from whole supernatants were concentrated and partially purified by using a copper-charged immobilized metal ion affinity chromatography column, confirming the affinity of these proteins for copper. A comparison of cell pellets and supernatants demonstrated that CuBP1 was more concentrated in supernatants than in cells. Our data are consistent with a model for a novel mechanism of copper detoxification in which excretion of copper-binding protein is induced by copper.

This article has been cited by other articles:

• Mason, M. G., Ball, A. S., Reeder, B. J., Silkstone, G., Nicholls, P., Wilson, M. T. (2001). Extracellular Heme Peroxidases in Actinomycetes: a Case of Mistaken Identity. Appl. Environ. Microbiol. 67: 4512-4519 [Abstract] [Full Text]  
• Bridge, T. A. M., White, C., Gadd, G. M. (1999). Extracellular metal-binding activity of the sulphate-reducing bacterium Desulfococcus multivorans. Microbiology 145: 2987-2995 [Abstract] [Full Text]