This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rho, J.
Right arrow Articles by Im, D.-S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rho, J.
Right arrow Articles by Im, D.-S.

 Previous Article  |  Next Article 

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.


This article has been cited by other articles:

  • Lei, N.-z., Zhang, X.-y., Chen, H.-z., Wang, Y., Zhan, Y.-y., Zheng, Z.-h., Shen, Y.-m., Wu, Q. (2009). A feedback regulatory loop between methyltransferase PRMT1 and orphan receptor TR3. Nucleic Acids Res 37: 832-848 [Abstract] [Full Text]  
  • Shire, K., Kapoor, P., Jiang, K., Hing, M. N. T., Sivachandran, N., Nguyen, T., Frappier, L. (2006). Regulation of the EBNA1 Epstein-Barr Virus Protein by Serine Phosphorylation and Arginine Methylation.. J. Virol. 80: 5261-5272 [Abstract] [Full Text]  
  • Dolzhanskaya, N., Merz, G., Aletta, J. M., Denman, R. B. (2006). Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP.. J. Cell Sci. 119: 1933-1946 [Abstract] [Full Text]  
  • Quer, J., Esteban, J. I., Cos, J., Sauleda, S., Ocana, L., Martell, M., Otero, T., Cubero, M., Palou, E., Murillo, P., Esteban, R., Guardia, J. (2005). Effect of Bottlenecking on Evolution of the Nonstructural Protein 3 Gene of Hepatitis C Virus during Sexually Transmitted Acute Resolving Infection. J. Virol. 79: 15131-15141 [Abstract] [Full Text]  
  • Duong, F. H. T., Christen, V., Berke, J. M., Penna, S. H., Moradpour, D., Heim, M. H. (2005). Upregulation of Protein Phosphatase 2Ac by Hepatitis C Virus Modulates NS3 Helicase Activity through Inhibition of Protein Arginine Methyltransferase 1. J. Virol. 79: 15342-15350 [Abstract] [Full Text]  
  • Hidajat, R., Nagano-Fujii, M., Deng, L., Tanaka, M., Takigawa, Y., Kitazawa, S., Hotta, H. (2005). Hepatitis C virus NS3 protein interacts with ELKS-{delta} and ELKS-{alpha}, members of a novel protein family involved in intracellular transport and secretory pathways. J. Gen. Virol. 86: 2197-2208 [Abstract] [Full Text]  
  • Komyod, W., Bauer, U.-M., Heinrich, P. C., Haan, S., Behrmann, I. (2005). Are STATS Arginine-methylated?. J. Biol. Chem. 280: 21700-21705 [Abstract] [Full Text]  
  • Boisvert, F.-M., Chenard, C. A., Richard, S. (2005). Protein Interfaces in Signaling Regulated by Arginine Methylation. Sci Signal 2005: re2-re2 [Abstract] [Full Text]  
  • Kim, J. W., Seo, M. Y., Shelat, A., Kim, C. S., Kwon, T. W., Lu, H.-h., Moustakas, D. T., Sun, J., Han, J. H. (2002). Structurally Conserved Amino Acid W501 Is Required for RNA Helicase Activity but Is Not Essential for DNA Helicase Activity of Hepatitis C Virus NS3 Protein. J. Virol. 77: 571-582 [Abstract] [Full Text]  
  • Li, H., Park, S., Kilburn, B., Jelinek, M. A., Henschen-Edman, A., Aswad, D. W., Stallcup, M. R., Laird-Offringa, I. A. (2002). Lipopolysaccharide-induced Methylation of HuR, an mRNA-stabilizing Protein, by CARM1. J. Biol. Chem. 277: 44623-44630 [Abstract] [Full Text]  
  • Frankel, A., Yadav, N., Lee, J., Branscombe, T. L., Clarke, S., Bedford, M. T. (2002). The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity. J. Biol. Chem. 277: 3537-3543 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»