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J. Biol. Chem., Vol. 283, Issue 50, 35186-35198, December 12, 2008

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Recruitment of the RNA Helicase RHAU to Stress Granules via a Unique RNA-binding Domain^*

Kateina Chalupníková, Simon Lattmann, Nives Selak, Fumiko Iwamoto¹, Yukio Fujiki, and Yoshikuni Nagamine²

From the Friedrich Miescher Institute for Biomedical Research, Novartis Research Foundation, Maulbeerstrasse 66, 4058 Basel, Switzerland and the Department of Biology, Faculty of Science, Kyushu University, Fukuoka 812-8581, Japan

In response to environmental stress, the translation machinery of cells is reprogrammed. The majority of actively translated mRNAs are released from polysomes and driven to specific cytoplasmic foci called stress granules (SGs) where dynamic changes in protein-RNA interaction determine the subsequent fate of mRNAs. Here we show that the DEAH box RNA helicase RHAU is a novel SG-associated protein. Although RHAU protein was originally identified as an AU-rich element-associated protein involved in urokinase-type plasminogen activator mRNA decay, it was not clear whether RHAU could directly interact with RNA. We have demonstrated that RHAU physically interacts with RNA in vitro and in vivo through a newly identified N-terminal RNA-binding domain, which was found to be both essential and sufficient for RHAU localization in SGs. We have also shown that the ATPase activity of RHAU plays a role in the RNA interaction and in the regulation of protein retention in SGs. Thus, our results show that RHAU is the fourth RNA helicase detected in SGs, after rck/p54, DDX3, and eIF4A, and that its association with SGs is dynamic and mediated by an RHAU-specific RNA-binding domain.

Received for publication, June 25, 2008 , and in revised form, September 16, 2008.

^* This work was supported in part by CREST grant (to Y. F.) from The Science and Technology Agency of Japan. 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 Figs. 1 and 2.

¹ Present address: Takara Bio Inc., Seta 3-4-1, Otsu, Shiga 520-2134, Japan.

² To whom correspondence should be addressed. Tel.: 41-61-697-6669; Fax: 41-61-697-3976; E-mail: Yoshikuni.nagamine{at}fmi.ch.

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