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The H1 double-stranded RNA genome of Ustilago maydis virus-H1 encodes a polyprotein that contains structural motifs for capsid polypeptide, papain-like protease, and RNA-dependent RNA polymerase

Cited 25 time in Web of Science Cited 29 time in Scopus
Authors
Kang, Jeong-Gu; Wu, Jae-Chang; Bruenn, Jeremy A.; Park, Chung-Mo
Issue Date
2001-08
Citation
Virus Research, Vol.76 No.2, pp.183-189
Keywords
double-stranded RNApolyproteinRNA-dependent RNA polymeraseUstilago maydis virus-H1 (UmV-H1)viral papain-like protease
Abstract
The Ustilago maydis viral (UmV) genome consists of I:three distinct size groups of double-stranded RNA (dsRNA) segment H (heavy), M (medium), and L (light). The H segments have been suggested to encode all essential viral proteins, but without ally molecular evidences. As a preliminary step to understand viral genomic organization and the molecular mechanism governing gene expression in UmV, we determined the complete nucleotide sequence of the H1 dsRNA genome in P1 viral killer subtype. The H1 dsRNA genome (designated UmV-H1) contained a single open reading Frame that encodes a polyprotein of 1820 residues, which is predicted to be autocatalytically processed by a viral papain-like protease to generate viral proteins. The amino-terminal region is the capsid polypeptide with a predicted molecular mass of 79.9 kDa. The carboxy-terminal region is the RNA-dependent RNA polymerase (RDRP) that has a high sequence homology to those of the totiviruses. The H2 dsRNA also encodes a distinct RDRP, suggesting that UmV is a complex virus system like the Saccharomyces cerevisiae viruses ScV-L1 and -La. (C) 2001 Elsevier Science B.V. All rights reserved.
ISSN
0168-1702
URI
https://hdl.handle.net/10371/172102
DOI
https://doi.org/10.1016/S0168-1702(01)00250-7
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College of Natural Sciences (자연과학대학)Dept. of Chemistry (화학부)Journal Papers (저널논문_화학부)
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