JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 Tsai, M.-S.
Right arrow Articles by Lin, N.-S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsai, M.-S.
Right arrow Articles by Lin, N.-S.

 Previous Article  |  Next Article 

Journal of Virology, April 1999, p. 3032-3039, Vol. 73, No. 4
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Bamboo Mosaic Potexvirus Satellite RNA (satBaMV RNA)-Encoded P20 Protein Preferentially Binds to satBaMV RNA

Ming-Shiun Tsai,1,2 Yau-Heiu Hsu,3 and Na-Sheng Lin1,2,*

Graduate Institute of Life Science, National Defence Medical Center, Taipei, Taiwan 100,1 Institute of Botany, Academia Sinica, Taipei, Taiwan 115,2 and Institute of Agricultural Biotechnology, National Chung Hsing University, Taichung 402,3 Republic of China

Received 14 May 1998/Accepted 29 December 1998

A satellite RNA of 836 nucleotides [excluding the poly(A) tail] depends on the bamboo mosaic potexvirus (BaMV) for its replication and encapsidation. The BaMV satellite RNA (satBaMV) contains a single open reading frame encoding a 20-kDa nonstructural protein (P20). The P20 protein with eight histidine residues at the C terminus was overexpressed in Escherichia coli. Experiments of gel retardation, UV cross-linking, and Northwestern hybridization demonstrated that purified P20 was a nucleic-acid-binding protein. The binding of P20 to nucleic acids was strong and highly cooperative. P20 preferred binding to satBaMV- or BaMV-related sequences rather than to nonrelated sequences. By deletion analysis, the P20 binding sites were mainly located at the 5' and 3' untranslated regions of satBaMV RNA, and the RNA-protein interactions could compete with the poly(G) and, less efficiently, with the poly(U) homopolymers. The N-terminal arginine-rich motif of P20 was the RNA binding domain, as shown by in-frame deletion analysis. This is the first report that a plant virus satellite RNA-encoded nonstructural protein preferentially binds with nucleic acids.

* Corresponding author. Mailing address: Institute of Botany, Academia Sinica, Taipei, Taiwan 115, Republic of China. Phone: 886-2-2789-9590, ext. 124. Fax: 886-2-2782-7954. E-mail: nslin{at}ccvax.sinica.edu.tw.

Journal of Virology, April 1999, p. 3032-3039, Vol. 73, No. 4
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 1999 by the American Society for Microbiology. All rights reserved.