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Originally published In Press as doi:10.1074/jbc.M006892200 on November 28, 2000

J. Biol. Chem., Vol. 276, Issue 8, 5445-5451, February 23, 2001
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A Role of RNA Helicase A in cis-Acting Transactivation Response Element-mediated Transcriptional Regulation of Human Immunodeficiency Virus Type 1*

Ryouji FujiiDagger , Mika Okamoto§, Satoko ArataniDagger , Takayuki OishiDagger , Takayuki OhshimaDagger , Kazunari TairaDagger , Masanori Baba§, Akiyoshi FukamizuDagger ||, and Toshihiro NakajimaDagger ||**Dagger Dagger

From the Dagger  Institute of Applied Biochemistry, || Center for Tsukuba Advanced Research Alliance, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba, Ibaraki 305-8577, the § Division of Human Retroviruses, Center for Chronic Viral Diseases, Faculty of Medicine, Kagoshima University, 8-35-1, Sakuragaoka, Kagoshima 890-8520, and ** PRESTO, Japan Science and Technology Corporation, 4-1-8 Honcho, Kawaguchi, Saitama, 332-0012, Japan

RNA helicase A (RHA) has two double-stranded (ds) RNA-binding domains (dsRBD1 and dsRBD2). These domains are conserved with the cis-acting transactivation response element (TAR)-binding protein (TRBP) and dsRNA-activated protein kinase (PKR). TRBP and PKR are involved in the regulation of HIV-1 gene expression through their binding to TAR RNA. This study shows that RHA also plays an important role in TAR-mediated HIV-1 gene expression. Wild-type RHA preferably bound to TAR RNA in vitro and in vivo. Overexpression of wild type RHA strongly enhanced viral mRNA synthesis and virion production as well as HIV-1 long terminal repeat-directed reporter (luciferase) gene expression. Substitution of lysine for glutamate at residue 236 in dsRBD2 (RHAK236E) reduced its affinity for TAR RNA and impaired HIV-1 transcriptional activity. These results indicate that TAR RNA is a preferred target of RHA dsRBDs and that RHA enhances HIV-1 transcription in vivo in part through the TAR-binding of RHA.

* This work was supported by grants from the Japanese Ministry of Education, Science, Culture, and Sports (10480196 and 10177230), Japanese Ministry of Health and Welfare, Japan Science and Technology Corporation (PRESTO), Human Health Science Foundation Medicitial Welfide Foundation, and by funds from Memorial Yamanouchi Foundation, Kaken Pharmaceutical Co. Ltd., and Santen Pharmaceutical Co. Ltd.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Dept. of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Tokyo 113-8656, Japan.

Dagger Dagger To whom correspondence should be addressed: Department of Genome Science, Institute of Medical Science, St. Marianna University of Medicine, 2-16-1 Sugao, Miyamae-ku, Kawasaki Kanagawa 216-8512, Japan. Tel.: 81-44-977-8111 (ext. 4113); Fax: 81-44-975-4599; E-mail: nakashit@marianna-u-ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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