HspA and HtpG enhance thermotolerance in the cyanobacterium, Microcystis aeruginosa NIES-298

J Microbiol Biotechnol. 2012 Jan;22(1):118-25. doi: 10.4014/jmb.1108.08001.

Abstract

Heat shock proteins (Hsps) play a key role in the cellular defense response to diverse environmental stresses. Here, the role of Hsp genes in the acquisition of thermotolerance in the cyanobacterium Microcystis aeruginosa NIES-298 was investigated. Twelve Hsp-related genes were examined to observe their modulated expression patterns at different temperatures (10, 15, 25, and 35° C) over different exposure periods. HspA and HtpG transcripts showed an up-regulation of expression at low temperatures (10 and 15° C) and high temperature (35° C), compared with the control (25° C). To examine their effects upon thermotolerance, we purified recombinant HspA and HtpG proteins. During a thermotolerance study at 54° C, the HspA-transformed bacteria showed increased thermotolerance compared with the control. HtpG also played a role in the defense response to acute heat stress within 30 min. These findings provide a better understanding of cellular protection mechanisms against heat stress in cyanobacteria.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cold Temperature
  • Gene Expression Profiling*
  • HSP90 Heat-Shock Proteins / genetics
  • HSP90 Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism*
  • Hot Temperature
  • Microbial Viability / radiation effects
  • Microcystis / genetics
  • Microcystis / physiology*
  • Microcystis / radiation effects*
  • Recombinant Proteins / isolation & purification

Substances

  • Bacterial Proteins
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins
  • HspA protein, bacteria
  • Recombinant Proteins
  • HtpG protein, bacteria