Chromosome remodelling by SMC/Condensin in B. subtilis is regulated by monomeric Soj/ParA during growth and sporulation

Proc Natl Acad Sci U S A. 2022 Oct 11;119(41):e2204042119. doi: 10.1073/pnas.2204042119. Epub 2022 Oct 7.

Abstract

SMC complexes, loaded at ParB-parS sites, are key mediators of chromosome organization in bacteria. ParA/Soj proteins interact with ParB/Spo0J in a pathway involving adenosine triphosphate (ATP)-dependent dimerization and DNA binding, facilitating chromosome segregation in bacteria. In Bacillus subtilis, ParA/Soj also regulates DNA replication initiation and along with ParB/Spo0J is involved in cell cycle changes during endospore formation. The first morphological stage in sporulation is the formation of an elongated chromosome structure called an axial filament. Here, we show that a major redistribution of SMC complexes drives axial filament formation in a process regulated by ParA/Soj. Furthermore, and unexpectedly, this regulation is dependent on monomeric forms of ParA/Soj that cannot bind DNA or hydrolyze ATP. These results reveal additional roles for ParA/Soj proteins in the regulation of SMC dynamics in bacteria and yet further complexity in the web of interactions involving chromosome replication, segregation and organization, controlled by ParAB and SMC.

Keywords: B. subtilis; ParABS; SMC/Condensin; chromosome segregation; sporulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases
  • Adenosine Triphosphate / metabolism
  • Bacillus subtilis* / metabolism
  • Bacterial Proteins / metabolism
  • Chromosome Segregation
  • Chromosomes, Bacterial* / genetics
  • Chromosomes, Bacterial* / metabolism
  • DNA, Bacterial / metabolism
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Multiprotein Complexes

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • Multiprotein Complexes
  • condensin complexes
  • Adenosine Triphosphate
  • Adenosine Triphosphatases