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Publication Detail

Title: Escherichia coli CopA N-terminal Cys(X)(2)Cys motifs are not required for copper resistance or transport.

Authors: Fan, B; Grass, G; Rensing, C; Rosen, B P

Published In Biochem Biophys Res Commun, (2001 Aug 17)

Abstract: Escherichia coli CopA is a Cu(I)-translocating P-type ATPase that is involved in copper export and resistance. It is an orthologue of the human Menkes and Wilson disease-related proteins. Each of those two human copper pumps has six N-terminal Cys(X)(2)Cys sequences, but their function in transport is unclear. CopA has two N-terminal Cys(X)(2)Cys sequences, GLSC(14)GHC(17) and GMSC(110)ASC(113). The requirement of these cysteine motifs was investigated by mutagenesis of the codons for all four cysteine residues, singly and in combination. Cells of a copA deletion strain expressing genes for the mutant genes were nearly as resistant to copper as the wild type. In addition, everted membrane vesicles from cells expressing the mutant copA genes exhibited ATP-coupled accumulation of copper similar to that of the wild type. The results indicate that neither of two N-terminal Cys(X)(2)Cys motifs is required for either resistance or transport.

PubMed ID: 11500054 Exiting the NIEHS site

MeSH Terms: Adenosine Triphosphate/physiology; Amino Acid Motifs; Bacterial Proteins/chemistry*; Bacterial Proteins/genetics; Biological Transport; Copper/metabolism; Copper/pharmacology*; Cysteine/genetics; Cytoplasmic Vesicles/metabolism; Escherichia coli/drug effects*; Mutagenesis, Site-Directed; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.

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