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Heat shock proteins are families of proteins which display an enhanced expression in response to heat shock or other stresses. Heat shock proteins are ubiquitous, and their primary sequences are highly conserved among different species. Many heat shock proteins are molecular chaperones and play essential roles in protein folding, repair, translocation, and degradation. Cyanobacteria are photoautotrophic prokaryotes whose habitats are extensive, indicating that they have adapted to various environmental conditions. Heat shock proteins may well have been playing important roles in their successful adaptation. We cloned genes encoding HtpG and small HSP from cyanobacteria. Inactivation of the htpG gene resulted in a decrease in the cell’s ability to develop thermo-tolerance (i.e., acquired thermo-tolerance), while over-production of small HSP increased the basal thermo-tolerance which is estimated by cell survival after a sudden lethal temperature treatment. In contrast to cyanobacteria, heterotrophic prokaryotes such as E. coli and B. subtilis, phenotypes of the htpG and small HSP mutants are not clear. Recently, we cloned a novel heat shock gene, orf7.5, which encodes a polypeptide of 63 amino acids. The inactivation of the gene led to a decrease in the cyanobacterial basal and acquired thermo-tolerances. Accumulation of the groEL transcript in the orf7.5 mutant was strongly reduced. We postulate that the Orf7.5 protein together with the major sigma factor interacts with the groEL gene to regulate its heat induction.
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