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

• Published in: Virus research 2001-08, Vol.76 (2), p.183-189
• Main Authors: Kang, Jeong-Gu, Wu, Jae-Chang, Bruenn, Jeremy A., Park, Chung-Mo
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Base Sequence; Capsid - genetics; DNA, Viral; Double-stranded RNA; Genome, Viral; Molecular Sequence Data; Papain - genetics; Peptides - genetics; Polyprotein; polyproteins; Polyproteins - genetics; RNA Replicase - genetics; RNA Viruses - genetics; RNA, Double-Stranded - analysis; RNA, Viral - analysis; RNA-dependent RNA polymerase; Ustilago - virology; Ustilago maydis virus; Ustilago maydis virus-H1 (UmV-H1); Viral papain-like protease
• ISSN: 0168-1702; 1872-7492
• DOI: 10.1016/S0168-1702(01)00250-7

The Ustilago maydis viral (UmV) genome consists of three distinct size groups of double-stranded RNA (dsRNA) segments: H (heavy), M (medium), and L (light). The H segments have been suggested to encode all essential viral proteins, but without any 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.