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Originally published In Press as doi:10.1074/jbc.M609545200 on December 6, 2006
J. Biol. Chem., Vol. 282, Issue 6, 3605-3613, February 9, 2007
Role of Heat Stress Transcription Factor HsfA5 as Specific Repressor of HsfA4*
Sanjeev K. Baniwal,
Kwan Yu Chan,
Klaus-Dieter Scharf, and
Lutz Nover1
From the
Department of Molecular Cell Biology, Biocenter of the Goethe University, Max-von-Laue-Str. 9, D-60438 Frankfurt/M., Germany
Unlike other eukaryotes, plants possess a complex family of heat stress transcription factors (Hsfs) with usually more than 20 members. Among them, Hsfs A4 and A5 form a group distinguished from other Hsfs by structural features of their oligomerization domains and by a number of conserved signature sequences. We show that A4 Hsfs are potent activators of heat stress gene expression, whereas A5 Hsfs act as specific repressors of HsfA4 activity. The oligomerization domain of HsfA5 alone is necessary and sufficient to exert this effect. Due to the high specificity of the oligomerization domains, other class A Hsfs are not affected. Pull-down assay and yeast two-hybrid interaction tests demonstrate that the tendency to form HsfA4/A5 heterooligomers is stronger than the formation of homooligomers. The specificity of interaction between Hsfs A4 and A5 was confirmed by bimolecular fluorescence complementation experiments. The major role of the representatives of the HsfA4/A5 group, which are not involved in the conventional heat stress response, may reside in cell type-specific functions connected with the control of cell death triggered by pathogen infection and/or reactive oxygen species.
Received for publication, October 10, 2006
, and in revised form, November 30, 2006.
* This work was supported by grants to LN from the Deutsche Forschungsgemeinschaft (No 249/4). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental tables and figures.
1 To whom correspondence should be addressed. E-mail: nover{at}cellbiology.uni-frankfurt.de.

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Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.
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