title: Membrane topology of the Escherichia coli AmpG permease required for recycling of cell wall anhydromuropeptides and AmpC beta-lactamase induction.
abstract: 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 beta-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 beta-lactamase fusion. In the proposed model, AmpG contains 10 transmembrane segments and two large cytoplasmic loops.
authors.affiliation: Départment de Biologie, Faculté des Sciences, Université My Ismail, Meknès, Morocco.
authors.forename: Aicha
authors.initials: A
authors.lastname: Chahboune
authors.forename: Marc
authors.initials: M
authors.lastname: Decaffmeyer
authors.forename: Robert
authors.initials: R
authors.lastname: Brasseur
authors.forename: Bernard
authors.initials: B
authors.lastname: Joris
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000502:physiology; D001483:Base Sequence; D002462:Cell Membrane / Q000201:enzymology; D002473:Cell Wall / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000502:physiology; D008969:Molecular Sequence Data; D010457:Peptidoglycan / Q000378:metabolism*; D001618:beta-Lactamases / Q000096:biosynthesis
chemical_list: C084284:AmpG protein, Bacteria; D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D010457:Peptidoglycan; C048795:AmpC beta-lactamases; D001618:beta-Lactamases
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