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

被引：113

作者：

Cheng, QM ^{[1
]}

Park, JT ^{[1
]}

机构：

[1] Tufts Univ, Sch Med, Dept Mol Biol & Microbiol, Boston, MA 02111 USA

来源：

JOURNAL OF BACTERIOLOGY | 2002年 / 184卷 / 23期

关键词：

D O I：

10.1128/JB.184.23.6434-6436.2002

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：6434 / 6436

页数：3

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