title: Subunit Arrangement in GpsB, a Regulator of Cell Wall Biosynthesis.
abstract: GpsB, a key regulator of cell division in Gram-positive bacteria, interacts with a key peptidoglycan synthase at the cell division septum, the penicillin binding protein PBP1 (a.k.a. PonA). Bacillus subtilis GpsB has been reported to interact with other components of the cell division machinery, including EzrA, MreC, and PrkC. In this study, we report an analysis of the arrangement of subunits in Listeria monocytogenes GpsB by small-angle X-ray scattering. The resulting model has an elongated shape with residues critical for interaction with PBP1 and the cell membrane clustered at one end of the molecule. Mutations that destabilize the hexameric assembly of the wild-type protein have a gpsB null phenotype, indicating that oligomerization is critical for the correct function of GpsB. We suggest a model in which a single GpsB hexamer can interact with multiple PBP1 molecules and can therefore influence the arrangement of PBP1 molecules within the cell division machinery, a dynamic multiprotein complex called the divisome, consistent with a role for GpsB in modulating the synthesis of the cell wall.
authors.affiliation: 1 Institute for Cell and Molecular Biosciences, University of Newcastle , Newcastle upon Tyne, United Kingdom .
authors.forename: Robert M
authors.initials: RM
authors.lastname: Cleverley
authors.affiliation: 2 FG11 Division of Enteropathogenic Bacteria and Legionella, Robert Koch Institute , Wernigerode, Germany .
authors.forename: Jeanine
authors.initials: J
authors.lastname: Rismondo
authors.affiliation: 3 Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot , United Kingdom .|4 Wellcome Trust Centre for Cell Matrix Research, Faculty of Life Sciences, University of Manchester , Manchester, United Kingdom .
authors.forename: Michael P
authors.initials: MP
authors.lastname: Lockhart-Cairns
authors.affiliation: 5 Membrane Biochemistry and Biophysics, Bijvoet Centre for Biomolecular Research, University of Utrecht , Utrecht, the Netherlands .
authors.forename: Paulien T
authors.initials: PT
authors.lastname: Van Bentum
authors.affiliation: 6 Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, University of Newcastle , Newcastle upon Tyne, United Kingdom .
authors.forename: Alexander J F
authors.initials: AJ
authors.lastname: Egan
authors.affiliation: 6 Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, University of Newcastle , Newcastle upon Tyne, United Kingdom .
authors.forename: Waldemar
authors.initials: W
authors.lastname: Vollmer
authors.affiliation: 2 FG11 Division of Enteropathogenic Bacteria and Legionella, Robert Koch Institute , Wernigerode, Germany .
authors.forename: Sven
authors.initials: S
authors.lastname: Halbedel
authors.affiliation: 4 Wellcome Trust Centre for Cell Matrix Research, Faculty of Life Sciences, University of Manchester , Manchester, United Kingdom .
authors.forename: Clair
authors.initials: C
authors.lastname: Baldock
authors.affiliation: 5 Membrane Biochemistry and Biophysics, Bijvoet Centre for Biomolecular Research, University of Utrecht , Utrecht, the Netherlands .
authors.forename: Eefjan
authors.initials: E
authors.lastname: Breukink
authors.affiliation: 1 Institute for Cell and Molecular Biosciences, University of Newcastle , Newcastle upon Tyne, United Kingdom .
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Lewis
mesh_terms: D001412:Bacillus subtilis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D002455:Cell Division; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism*; D015870:Gene Expression; D008089:Listeria monocytogenes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D046915:Penicillin-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D046915:Penicillin-Binding Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins