Biomolecular NMR Assignments

, Volume 4, Issue 2, pp 235–238

1H, 13C and 15N resonance assignments of the major extracytoplasmic domain of the cell shape-determining protein MreC from Bacillus subtilis

  • Annika Kyburz
  • Vytautas Raulinaitis
  • Outi Koskela
  • Vesa Kontinen
  • Perttu Permi
  • Ilkka Kilpelainen
  • Raili Seppala
Article

DOI: 10.1007/s12104-010-9249-2

Cite this article as:
Kyburz, A., Raulinaitis, V., Koskela, O. et al. Biomol NMR Assign (2010) 4: 235. doi:10.1007/s12104-010-9249-2

Abstract

MreB, MreC and MreD are essential cell shape-determining morphogenetic proteins in Gram-positive and in Gram-negative bacteria. While MreB, the bacterial homologue of the eukaryotic cytoskeletal protein actin, has been extensively studied, the roles of MreC and MreD are less well understood. They both are transmembrane proteins. MreC has a predicted single transmembrane domain and the C-terminal part outside the cell membrane. MreC probably functions as a link between the intracellular cytoskeleton and the cell wall synthesizing machinery which is located at the outer surface of the cell membrane. Also proteins involved in cell wall synthesis participate in cell morphogenesis. How these two processes are coordinated is, however, poorly understood. Bacillus subtilis (BS), a non-pathogenic Gram-positive bacterium, is widely used as a model for Gram-positive pathogens, e.g. Staphylococcus aureus (SA). Currently, the structures of MreC from BS and SA are not known. As part of our efforts to elucidate the structure–function relationships of the morphogenetic protein complexes in Gram-positive bacteria, we present the backbone and side chain resonance assignments of the extracytoplasmic domain of MreC from BS.

Keywords

NMRAssignmentMreCBacillus subtilisCell shape-determining protein

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Annika Kyburz
    • 1
  • Vytautas Raulinaitis
    • 2
  • Outi Koskela
    • 1
  • Vesa Kontinen
    • 3
  • Perttu Permi
    • 2
  • Ilkka Kilpelainen
    • 1
  • Raili Seppala
    • 2
  1. 1.Laboratory of Organic Chemistry, Department of ChemistryUniversity of HelsinkiHelsinkiFinland
  2. 2.Program in Structural Biology and Biophysics, Institute of BiotechnologyUniversity of HelsinkiHelsinkiFinland
  3. 3.Antimicrobial Resistance Unit, Department of Infectious Disease Surveillance and ControlNational Institute for Health and Welfare (THL), PL 30HelsinkiFinland