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

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

NMR Assignment MreC Bacillus subtilis Cell shape-determining protein 

References

  1. Daniel RA, Errington J (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113:767–776CrossRefGoogle Scholar
  2. Divakaruni AV, Loo RR, Xie Y, Loo JA, Gober JW (2005) The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. Proc Natl Acad Sci U S A 102(51):18602–18607CrossRefADSGoogle Scholar
  3. Figge RM, Divakaruni AV, Gober JW (2004) MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Mol Microbiol 51(5):1321–1332CrossRefGoogle Scholar
  4. Goddard TD, Kneller DG (2004) Sparky 3. University of California, San FranciscoGoogle Scholar
  5. Hackbarth CJ, Kocagoz T, Kocagoz S, Chambers HF (1994) Point mutations in Staphylococcus aureus PBP 2 gene affect penicillin-binding kinetics and are associated with resistance. Antimicrob Agents Chemother 39(1):103–106Google Scholar
  6. Jones LJ, Carballido-López R, Errington J (2001) Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104(6):913–922CrossRefGoogle Scholar
  7. Kruse T, Bork-Jensen J, Gerdes K (2005) The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol Microbiol 55(1):78–89CrossRefGoogle Scholar
  8. Leaver M, Errington J (2005) Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis. Mol Microbiol 57(5):1196–1209CrossRefGoogle Scholar
  9. Lee JC, Stewart GC (2003) Essential Nature of the mreC Determinant of Bacillus subtilis. J Bacteriol 185(15):4490–4498CrossRefGoogle Scholar
  10. Permi P, Annila A (2004) Coherence transfer in proteins. Prog Nucl Magn Reson Spectrosc 44:97–137CrossRefGoogle Scholar
  11. Rice LB (2006) Antimicrobial resistance in gram-positive bacteria. Am J Infect Control 34(5):S11–S19CrossRefMathSciNetGoogle Scholar
  12. Tossavainen H, Permi P, Purhonen SL, Sarvas M, Kilpelainen I, Seppala R (2006) NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis. FEBS Lett 580:1822–1826CrossRefGoogle Scholar
  13. van den Ent F, Leaver M, Bendezu F, Errington J, de Boer P, Löwe J (2006) Dimeric structure of the cell shape protein MreC and its functional implications. Mol Microbiol 62(6):1631–1642CrossRefGoogle Scholar
  14. Varley AW, Stewart GC (1992) The divIVB region of the bacillus subtilis chromosome encodes homologs of escherichia coli septum placement (MinCD) and cell shape (MreBCD) determinants. J Bacteriol 174(21):6729–6742Google Scholar
  15. Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Bio NMR 4:171–180Google Scholar
  16. Wishart DS, Sykes BD, Richards FM (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647–1651CrossRefGoogle Scholar

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

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