Abstract
In cyanobacteria, a disruptant of hspA encoding a small heat shock protein homologue, shows decreased cell growth rates at moderately high temperatures, and loss of both basal and acquired thermo-tolerances, which resemble the phenotype of an htpG disruptant. In vitro studies have shown that both small heat shock protein and Hsp90 can bind and keep non-native proteins in a refolding-competent state under denaturing conditions. The aim of the present study is to elucidate whether constitutive expression of HspA can functionally replace HtpG, a prokaryotic homolog of Hsp90, in the cyanobacterium Synechococcus sp. PCC 7942. HspA did not improve the viability of the htpG disruptant at a lethal temperature, although it did that of the wild type. It did not improve an iron-starved phenotype of the mutant under normal growth conditions, a novel phenotype found in the present study. These results suggest that cellular function of HtpG may differ significantly from that of HspA.
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Acknowledgments
This work was supported in part by a Grant-in-aid for Scientific Research (C) (no. 16570028) from the Ministry of Education, Science, Sports and Culture of Japan to H. Nakamoto.
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Kojima, K., Nakamoto, H. Constitutive Expression of Small Heat Shock Protein in an htpG Disruptant of the Cyanobacterium Synechococcus sp. PCC 7942. Curr Microbiol 50, 272–276 (2005). https://doi.org/10.1007/s00284-005-4486-9
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DOI: https://doi.org/10.1007/s00284-005-4486-9