Caulobacter chromosome segregation is an ordered multistep process

Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14194-8. doi: 10.1073/pnas.1005274107. Epub 2010 Jul 26.

Abstract

Despite its fundamental nature, bacterial chromosome segregation remains poorly understood. Viewing segregation as a single process caused multiple proposed mechanisms to appear in conflict and failed to explain how asymmetrically dividing bacteria break symmetry to move only one of their chromosomes. Here, we demonstrate that the ParA ATPase extends from one cell pole and pulls the chromosome by retracting upon association with the ParB DNA-binding protein. Surprisingly, ParA disruption has a specific effect on chromosome segregation that only perturbs the latter stages of this process. Using quantitative high-resolution imaging, we demonstrate that this specificity results from the multistep nature of chromosome translocation. We propose that Caulobacter chromosome segregation follows an ordered pathway of events with distinct functions and mechanisms. Initiation releases polar tethering of the origin of replication, distinction spatially differentiates the two chromosomes, and commitment irreversibly translocates the distal centromeric locus. Thus, much as eukaryotic mitosis involves a sequence of distinct subprocesses, Caulobacter cells also segregate their chromosomes through an orchestrated series of steps. We discuss how the multistep view of bacterial chromosome segregation can help to explain and reconcile outstanding puzzles and frame future investigation.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphatases / physiology
  • Bacterial Proteins
  • Caulobacter / genetics*
  • Chromosome Segregation*
  • Chromosomes, Bacterial*
  • DNA-Binding Proteins / metabolism
  • DNA-Binding Proteins / physiology

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Adenosine Triphosphatases