ClpP-dependent and -independent activities encoded by the polycistronic clpK-encoding locus contribute to heat shock survival in Klebsiella pneumoniae

Res Microbiol. 2013 Apr;164(3):205-10. doi: 10.1016/j.resmic.2012.11.005. Epub 2012 Nov 28.

Abstract

The family of Clp ATPases plays an important role in bacterial physiology. Here we characterize the genetic locus encompassing a newly described plasmid-encoded ClpK protein protecting Klebsiella pneumoniae cells during heat shock. We demonstrate that the clpK gene is located in a polycistronic operon and that the variable downstream gene content correlates with heat-resistant phenotypes of different isolates. ClpK is encoded by a multifunctional transcriptional unit characterized by both ClpP-dependent and -independent activities. Notably, our data show that ClpP is indispensible for thermoprotection exerted by ClpK alone, suggesting that ClpK is a new member of the family of ClpP-interacting Clp ATPases.

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Endopeptidase Clp / genetics*
  • Gene Expression Regulation, Bacterial
  • Genes, Bacterial
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Response / genetics*
  • Hot Temperature
  • Klebsiella pneumoniae / genetics*
  • Klebsiella pneumoniae / metabolism*
  • Microbial Viability
  • Operon / genetics
  • Phenotype
  • Plasmids

Substances

  • Bacterial Proteins
  • Heat-Shock Proteins
  • Endopeptidase Clp