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Journal of Virology, September 2001, p. 8031-8044, Vol. 75, No. 17
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.17.8031-8044.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The Arginine-1493 Residue in QRRGRTGR1493G Motif IV of the Hepatitis C Virus NS3 Helicase Domain Is Essential for NS3 Protein Methylation by the Protein Arginine Methyltransferase 1

Jaerang Rho,1 Seeyoung Choi,1 Young Rim Seong,1 Joonho Choi,2 and Dong-Soo Im1,*

Cell Biology Laboratory, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejeon 305-333,1 and Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejeon,2 Republic of Korea

Received 20 October 2000/Accepted 23 May 2001

The NS3 protein of hepatitis C virus (HCV) contains protease and RNA helicase activities, both of which are likely to be essential for HCV propagation. An arginine residue present in the arginine-glycine (RG)-rich region of many RNA-binding proteins is posttranslationally methylated by protein arginine methyltransferases (PRMTs). Amino acid sequence analysis revealed that the NS3 protein contains seven RG motifs, including two potential RG motifs in the 1486-QRRGRTGRG-1494 motif IV of the RNA helicase domain, in which arginines are potentially methylated by PRMTs. Indeed, we found that the full-length NS3 protein is arginine methylated in vivo. The full-length NS3 protein and the NS3 RNA helicase domain were methylated by a crude human cell extract. The purified PRMT1 methylated the full-length NS3 and the RNA helicase domain, but not the NS3 protease domain. The NS3 helicase bound specifically and comigrated with PRMT1 in vitro. Mutational analyses indicate that the Arg1493 in the QRR1488GRTGR1493G region of the NS3 RNA helicase is essential for NS3 protein methylation and that Arg1488 is likely methylated. NS3 protein methylation by the PRMT1 was decreased in the presence of homoribopolymers, suggesting that the arginine-rich motif IV is involved in RNA binding. The results suggest that an arginine residue(s) in QRXGRXGR motif IV conserved in the virus-encoded RNA helicases can be posttranslationally methylated by the PRMT1.

* Corresponding author. Mailing address: Cell Biology Laboratory, Korea Research Institute of Bioscience and Biotechnology, Yusong, Taejeon 305-333, Republic of Korea. Phone: 82 42 860 4172. Fax: 82 42 860 4597. E-mail: imdongsu{at}mail.kribb.re.kr.

Journal of Virology, September 2001, p. 8031-8044, Vol. 75, No. 17
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.17.8031-8044.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.