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J. Biol. Chem., Vol. 282, Issue 14, 10333-10340, April 6, 2007

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Different Mechanisms Are Involved in the Transcriptional Activation by Yeast Heat Shock Transcription Factor through Two Different Types of Heat Shock Elements^*

From the Division of Health Sciences, Graduate School of Medical Science, Kanazawa University, 5-11-80 Kodatsuno, Kanazawa, Ishikawa 920-0942, Japan

The hydrophobic repeat is a conserved structural motif of eukaryotic heat shock transcription factor (HSF) that enables HSF to form a homotrimer. Homotrimeric HSF binds to heat shock elements (HSEs) consisting of three inverted repeats of the sequence nGAAn. Sequences consisting of four or more nGAAn units are bound cooperatively by two HSF trimers. We show that in Saccharomyces cerevisiae cells oligomerization-defective Hsf1 is not able to bind HSEs with three units and is not extensively phosphorylated in response to stress; it is therefore unable to activate genes containing this type of HSE. Several lines of evidence indicate that oligomerization is a prerequisite for stress-induced hyperphosphorylation of Hsf1. In contrast, oligomerization and hyperphosphorylation are not necessary for gene activation via HSEs with four units. Intragenic suppressor screening of oligomerization-defective hsf1 showed that an interface between adjacent DNA-binding domains is important for the binding of Hsf1 to the HSE. We suggest that Saccharomyces cerevisiae HSEs with different structures are regulated differently; HSEs with three units require Hsf1 to be both oligomerized and hyperphosphorylated, whereas HSEs with four or more units do not require either.

Received for publication, October 16, 2006 , and in revised form, February 6, 2007.

^* This work was supported in part by grants-in-aid for scientific research from the Ministry of Education, Sciences, Sports, and Culture (to H. S.). 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 3 supplemental figures.

¹ Present address: Dept. of Life Science, Faculty of Science, Okayama University of Science, 1-1 Ridaicho, Okayama 700-0005, Japan.

² To whom correspondence should be addressed. Tel.: 81-76-265-2588; Fax: 81-76-234-4369; E-mail: sakurai{at}kenroku.kanazawa-u.ac.jp.

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