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Membrane Topology of the Escherichia coli AmpG Permease Required for Recycling of Cell Wall Anhydromuropeptides and AmpC ß-Lactamase Induction

Département de Biologie, Faculté des Sciences, Université My Ismail, Meknès, Morocco,¹ Centre de Biophysique Moléculaire Numérique, Faculté Universitaire des Sciences Agronomiques de Gembloux, Gembloux,² Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, Sart Tilman (Liège), Belgium³

Received 25 June 2004/ Returned for modification 28 August 2004/ Accepted 25 October 2004

Escherichia coli, and presumably most other gram-negative bacteria, possesses an efficient protein machinery for recycling its peptidoglycan during cell growth. The major recycled peptidoglycan product is N-acetylglucosamine-1,6-anhydro-N-acetylmuramic acid-tetrapeptide. Its uptake from the periplasm into the cytoplasm is carried out via the AmpG protein, an intrinsic membrane protein. In gram-negative bacteria carrying an ampC ß-lactamase-inducible gene on their chromosomes, the induction mechanism is directly linked to peptidoglycan recycling. After identification of the different putative hydrophobic segments by computing, the AmpG topology was experimentally determined by using ß-lactamase fusion. In the proposed model, AmpG contains 10 transmembrane segments and two large cytoplasmic loops.

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