title: 1H, 13C and 15N resonance assignments of the major extracytoplasmic domain of the cell shape-determining protein MreC from Bacillus subtilis.
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.
authors.affiliation: Laboratory of Organic Chemistry, Department of Chemistry, University of Helsinki, A.I. Virtasen Aukio 1, P.O. Box 55, 00014, Helsinki, Finland. annika.kyburz@helsinki.fi
authors.forename: Annika
authors.initials: A
authors.lastname: Kyburz
authors.forename: Vytautas
authors.initials: V
authors.lastname: Raulinaitis
authors.forename: Outi
authors.initials: O
authors.lastname: Koskela
authors.forename: Vesa
authors.initials: V
authors.lastname: Kontinen
authors.forename: Perttu
authors.initials: P
authors.lastname: Permi
authors.forename: Ilkka
authors.initials: I
authors.lastname: Kilpelainen
authors.forename: Raili
authors.initials: R
authors.lastname: Seppala
mesh_terms: D001412:Bacillus subtilis / Q000737:chemistry* / Q000166:cytology*; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D003593:Cytoplasm / Q000737:chemistry*; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D002247:Carbon Isotopes; C062061:MreC protein, Bacteria; D009587:Nitrogen Isotopes; D006859:Hydrogen