Isolation and characterization of topological specificity mutants of minD in Bacillus subtilis

M E Karoui, J Errington

Research output: Contribution to journalArticlepeer-review

Abstract

In rod-shaped bacteria such as Bacillus subtilis, division site selection is mediated by MinC and MinD, which together function as a division inhibitor. Topological specificity is imposed by DivIVA, which ensures that MinCD specifically inhibits division close to the cell poles, while allowing division at mid-cell. MinD plays a central role in this process, as it positions and activates MinC and is dependent on DivIVA for its own positioning at the poles. To investigate MinD activities further, we have constructed and analysed a collection of minD mutants. Mutations in the conserved ATPase motifs lead to an inactive protein, possibly unable to oligomerize, but which nevertheless retains some affinity for the cell membrane. Several mutations affecting the mid- to C-terminal parts of MinD led to a protein probably unable to interact with DivIVA, but that could still stimulate division inhibition by MinC. These findings suggest that the ATPase activity of MinD is necessary for all its functions (possibly in part by controlling the oligomerization state of the protein). The other mutations may identify a surface of MinD involved in its interactions with DivIVA and a possible mechanism for control of MinD by DivIVA.
Original languageEnglish
Pages (from-to)1211-21
Number of pages11
JournalMolecular Microbiology
Volume42
Issue number5
DOIs
Publication statusPublished - Dec 2001

Keywords

  • Protein Structure, Secondary
  • Bacillus subtilis
  • Cell Cycle Proteins
  • Recombinant Proteins
  • Models, Molecular
  • Amino Acid Sequence
  • Plasmids
  • Membrane Proteins
  • Protein Binding
  • Mutagenesis
  • Bacterial Proteins
  • Sequence Alignment
  • Escherichia coli Proteins
  • Molecular Sequence Data
  • Adenosine Triphosphatases
  • Sequence Homology, Amino Acid
  • Cell Division

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