Characterization of the mycobacterial chromosome segregation protein ParB and identification of its target in Mycobacterium smegmatis

Microbiology (Reading). 2007 Dec;153(Pt 12):4050-4060. doi: 10.1099/mic.0.2007/011619-0.

Abstract

Bacterial chromosomes (though not Escherichia coli and some other gamma-proteobacterial chromosomes) contain parS sequences and parAB genes encoding partitioning proteins, i.e. ParA (ATPase) and ParB (DNA-binding proteins) that are components of the segregation machinery. Here, mycobacterial parABS elements were characterized for the first time. parAB genes are not essential in Mycobacterium smegmatis; however, elimination or overexpression of ParB protein causes growth inhibition. Deletion of parB also leads to a rather severe chromosome segregation defect: up to 10% of the cells were anucleate. Mycobacterial ParB protein uses three oriC-proximal parS sequences as targets to organize the origin region into a compact nucleoprotein complex. Formation of such a complex involves ParB-ParB interactions and is assisted by ParA protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Chromosome Segregation*
  • Chromosomes, Bacterial / genetics*
  • Culture Media
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Gene Deletion
  • Gene Expression Regulation, Bacterial
  • Molecular Sequence Data
  • Mycobacterium smegmatis / genetics*
  • Mycobacterium smegmatis / growth & development
  • Mycobacterium smegmatis / metabolism
  • Mycobacterium tuberculosis / genetics
  • Mycobacterium tuberculosis / metabolism
  • Operon
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Replication Origin

Substances

  • Bacterial Proteins
  • Culture Media
  • DNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Adenosine Triphosphatases