NDLI: Recruitment of the RNA helicase RHAU to stress granules via a unique RNA-binding domain.

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Recruitment of the RNA helicase RHAU to stress granules via a unique RNA-binding domain.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fujiki, Yukio Lattmann, Simon Iwamoto, Fumiko Nagamine, Yoshikuni Chalupníková, Katerina Selak, Nives
Description	Author Affiliation: Chalupníková K ( Friedrich Miescher Institute for Biomedical Research, Novartis Research Foundation, Maulbeerstrasse 66, 4058 Basel, Switzerland.)
Abstract	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.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	50
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-12-12
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DEAD-box RNA Helicases Metabolism RNA Helicases Chemistry Adenosine Triphosphatases Amino Acid Sequence Cross-Linking Reagents Pharmacology Escherichia Coli Eukaryotic Initiation Factor-4A Fluorescence Recovery After Photobleaching HeLa Cells Kinetics Microscopy, Fluorescence Molecular Sequence Data Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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