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. 2002 Dec;184(23):6434-6.
doi: 10.1128/JB.184.23.6434-6436.2002.

Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides

Qiaomei Cheng  1 , James T Park
Affiliations

Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides

Qiaomei Cheng et al. J Bacteriol. 2002 Dec.

Abstract

AmpG was originally identified as a gene required for induction of beta-lactamase. Subsequently, we found AmpG to be a permease required for recycling of murein tripeptide and uptake of anhydro-muropeptides. We have now studied the specificity of the AmpG permease. The principal requirement is for the presence of the disaccharide, N-acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-anhMurNAc). These unique substrates for AmpG, which contain murein peptides linked to GlcNAc-anhMurNAc, are produced by turnover of the cell wall during logarithmic growth. AmpG permease is sensitive to carbonylcyanide m-chlorophenylhydrazone, demonstrating that AmpG permease is a single-component permease and that transport is dependent on the proton motive force.

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Figures

FIG. 1.
FIG. 1.
Uptake of various ligands by freeze-thawed cells of wild-type and ampG strains. *, labeled with 3H-Dap; all other ligands labeled with 3H-GlcNH2.
See this image and copyright information in PMC

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