MreB-Dependent Inhibition of Cell Elongation during the Escape from Competence in Bacillus subtilis

PLoS Genet. 2015 Jun 19;11(6):e1005299. doi: 10.1371/journal.pgen.1005299. eCollection 2015 Jun.

Abstract

During bacterial exponential growth, the morphogenetic actin-like MreB proteins form membrane-associated assemblies that move processively following trajectories perpendicular to the long axis of the cell. Such MreB structures are thought to scaffold and restrict the movement of peptidoglycan synthesizing machineries, thereby coordinating sidewall elongation. In Bacillus subtilis, this function is performed by the redundant action of three MreB isoforms, namely MreB, Mbl and MreBH. mreB and mbl are highly transcribed from vegetative promoters. We have found that their expression is maximal at the end of exponential phase, and rapidly decreases to a low basal level upon entering stationary phase. However, in cells developing genetic competence, a stationary phase physiological adaptation, expression of mreB was specifically reactivated by the central competence regulator ComK. In competent cells, MreB was found in complex with several competence proteins by in vitro pull-down assays. In addition, it co-localized with the polar clusters formed by the late competence peripheral protein ComGA, in a ComGA-dependent manner. ComGA has been shown to be essential for the inhibition of cell elongation characteristic of cells escaping the competence state. We show here that the pathway controlling this elongation inhibition also involves MreB. Our findings suggest that ComGA sequesters MreB to prevent cell elongation and therefore the escape from competence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / cytology
  • Bacillus subtilis / genetics*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cell Cycle
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • DNA Transformation Competence*
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism

Substances

  • Bacterial Proteins
  • Cytoskeletal Proteins
  • Protein Isoforms

Grants and funding

This work was supported by a Return Post-doctoral grant from the French National Research Agency (NM, ANR-12-PDOC-002, Cytostat); a starting grant from the European Research Council (RCL, ERCStG 311231, BaCeMo) and the EMBO Young Investigator program (RCL, EMBO YIP 2259). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.