title: Deformations in the cytoplasmic membrane of Escherichia coli direct the synthesis of peptidoglycan. The hernia model.
abstract: To explain the growth of the Gram-negative envelope and in particular how it could be strengthened where it is weakest, we propose in the hernia model that local weakening of the peptidoglycan sacculus allows turgor pressure to cause the envelope to bulge outwards in a hernia; the consequent local alteration in the radius of curvature of the cytoplasmic membrane causes local alterations in phospholipid structure and composition that determine both the synthesis and hydrolysis of peptidoglycan. This proposal is supported by evidence that phospholipid composition determines the activity of phospho-N-acetylmuramic acid pentapeptide translocase, UDP-N-acetylglucosamine:N-acetylmuramic acid-(pentapeptide)-P-P-bactoprenyl-N-acetylglucosamine transferase, bactoprenyl phosphate phosphokinase, and N-acetylmuramyl-L-alanine amidase. We also propose that the shape of Escherichia coli is maintained by contractile proteins acting at the hernia. Given the universal importance of membranes, these proposals have implications for the determination of shape in eukaryotic cells.
authors.affiliation: Department of Microbiology, University of Leicester, UK.
authors.forename: V
authors.initials: V
authors.lastname: Norris
authors.forename: B
authors.initials: B
authors.lastname: Manners
mesh_terms: D001426:Bacterial Proteins; D002352:Carrier Proteins; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure*; D004926:Escherichia coli / Q000378:metabolism* / Q000648:ultrastructure; D006602:Hexosyltransferases / Q000378:metabolism*; D008051:Lipid Bilayers; D008433:Mathematics; D008563:Membrane Lipids / Q000378:metabolism; D008961:Models, Structural; D008962:Models, Theoretical; D009097:Multienzyme Complexes / Q000378:metabolism*; D002267:Muramoylpentapeptide Carboxypeptidase; D009842:Oligopeptides / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010457:Peptidoglycan / Q000096:biosynthesis*; D010458:Peptidyl Transferases / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D008051:Lipid Bilayers; D008563:Membrane Lipids; D009097:Multienzyme Complexes; D009842:Oligopeptides; D046915:Penicillin-Binding Proteins; D010457:Peptidoglycan; D010743:Phospholipids; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase