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Journal of Biochemistry Advance Access published online on November 3, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp177
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Identification of the Phr-dependent heat shock regulon in the hyperthermophilic archaeon, Thermococcus kodakaraensis

Tamotsu Kanai1, Shogo Takedomi1, Shinsuke Fujiwara2, Haruyuki Atomi1 and Tadayuki Imanaka3

1 Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan
2 Department of Bioscience, School of Science and Technology, Kwansei-Gakuin University, 2-1 Gakuen, Sanda 669-1337, Japan.
3 Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Kusatsu 525-8577, Japan.

*To whom correspondence should be addressed: Tadayuki Imanaka Tel/Fax: +81-77-561-5811, E-mail: imanaka{at}sk.ritsumei.ac.jp

Received June 21, 2009; Accepted October 15, 2009


  Abstract

The hyperthermophilic archaeon Thermococcus kodakaraensis harbors a putative transcriptional regulator (Tk-Phr) that is orthologous to the Pyrococcus furiosus Phr (Pf-Phr). Pf-Phr, a transcriptional regulator, represses genes encoding the small heat shock protein (sHSP), AAA+ ATPase, and Pf-Phr itself under normal growth temperatures. Here we constructed a gene disruption strain of Tk-Phr (strain KHR1). KHR1 cells showed similar specific growth rates with those of the wild-type strain under various temperatures. A whole genome microarray analysis was performed between KHR1 and wild-type cells grown at 80°C. Transcript levels of more than 20 genes were significantly higher in KHR1 cells. Most genes contained a sequence motif virtually identical to that of Pf-Phr in their 5'-flanking regions. The Tk-Phr regulon included genes encoding sHSP, AAA+ ATPase, prefoldin, RecA superfamily ATPase, and Tip49. On the other hand, more than half of the members in the regulon encoded conserved/hypothetical proteins, raising the possibility that these proteins participate in unidentified processes of the heat shock response. In contrast, Tk-Phr deletion did not lead to dramatic increases in transcript and protein levels of a chaperonin (CpkB) previously shown to respond to heat shock, suggesting the presence of a second, Phr-independent heat shock response mechanism in T. kodakaraensis.

Key Words: archaea, heat shock response, microarray, Phr, transcriptional regulation


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