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Subunit Arrangement in GpsB, a Regulator of Cell Wall Biosynthesis

DOI: 10.1089/mdr.2016.0050 DOI Help

Authors: Robert M. Cleverley (Newcastle University) , Jeanine Rismondo (FG11 Division of Enteropathogenic Bacteria and Legionella, Robert Koch Institute) , Michael P. Lockhart (University of Manchester;l Diamond Light Source Ltd) , Paulien T. Van Bentum (Membrane Biochemistry and Biophysics, Bijvoet Centre for Biomolecular Research, University of Utrecht) , Alexander J. F. Egan , Waldemar Vollmer (Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, University of Newcastle) , Sven Halbedel (FG11 Division of Enteropathogenic Bacteria and Legionella, Robert Koch Institute) , Clair Baldock (University of Manchester) , Eefjan Breukink (5Membrane Biochemistry and Biophysics, Bijvoet Centre for Biomolecular Research, University of Utrecht) , Richard J. Lewis (1Institute for Cell and Molecular Biosciences, University of Newcastle)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Microbial Drug Resistance , VOL 22 , PAGES 446 - 460

State: Published (Approved)
Published: September 2016
Diamond Proposal Number(s): 1221

Open Access Open Access

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.

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: B21-High Throughput SAXS

Other Facilities: DESY

Documents:
mdr.2016.pdf