A role for the essential YycG sensor histidine kinase in sensing cell division

Mol Microbiol. 2011 Jan;79(2):503-22. doi: 10.1111/j.1365-2958.2010.07464.x. Epub 2010 Nov 29.

Abstract

The YycG sensor histidine kinase co-ordinates cell wall remodelling with cell division in Gram-positive bacteria by controlling the transcription of genes for autolysins and their inhibitors. Bacillus subtilis YycG senses cell division and is enzymatically activated by associating with the divisome at the division septum. Here it is shown that the cytoplasmic PAS domain of this multi-domain transmembrane kinase is a determining factor translocating the kinase to the division septum. Furthermore, translocation to the division septum, per se, is insufficient to activate YycG, indicating that specific interactions and/or ligands produced there are required to stimulate kinase activity. N-terminal truncations of YycG lose negative regulation of their activity inferring that this regulation is accomplished through its transmembrane and extramembrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome. The data indicate that YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI and its activation is co-ordinated to cell division in dividing cells by specific interactions that occur within the divisome.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / physiology*
  • Cell Division*
  • Histidine Kinase
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping
  • Protein Kinases / genetics
  • Protein Kinases / metabolism*
  • Sequence Deletion

Substances

  • Protein Kinases
  • Histidine Kinase