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.
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Acknowledgments
Annika Kyburz acknowledges The Finnish National Graduate School in Informational and Structural Biology (ISB). The work has been financially supported by the grants 122170 (to P. P) and 123318 (to I. K) from the Academy of Finland.
Ethical Standards
The experiments performed for this research comply with the current laws of Finland.
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The authors declare that they have no conflict of interests.
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Kyburz, A., Raulinaitis, V., Koskela, O. et al. 1H, 13C and 15N resonance assignments of the major extracytoplasmic domain of the cell shape-determining protein MreC from Bacillus subtilis. Biomol NMR Assign 4, 235–238 (2010). https://doi.org/10.1007/s12104-010-9249-2
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DOI: https://doi.org/10.1007/s12104-010-9249-2