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Journal of Bacteriology, December 2002, p. 6434-6436, Vol. 184, No. 23
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.23.6434-6436.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Substrate Specificity of the AmpG Permease Required for Recycling of Cell Wall Anhydro-Muropeptides

Qiaomei Cheng and James T. Park*

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111

Received 5 June 2002/ Accepted 6 September 2002

AmpG was originally identified as a gene required for induction of ß-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-ß-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.

* Corresponding author. Mailing address: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. Phone: (617) 636-6753. Fax: (617) 636-0337. E-mail: James.Park{at}tufts.edu.

Journal of Bacteriology, December 2002, p. 6434-6436, Vol. 184, No. 23
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.23.6434-6436.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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