Sindbis virus proteins nsP1 and nsP2 contain homology to nonstructural proteins from several RNA plant viruses.
Although the genetic organization of tobacco mosaic virus (TMV) differs considerably from that of the tripartite viruses (alfalfa mosaic virus [AlMV] and brome mosaic virus [BMV]), all of these RNA plant viruses share three domains of homology among their nonstructural proteins. One such domain, common to the AlMV and BMV 2a proteins and the readthrough portion of TMV p183, is also homologous to the readthrough protein nsP4 of Sindbis virus (Haseloff et al., Proc. Natl. Acad. Sci. U.S.A. 81:4358-4362, 1984). Two more domains are conserved among the AlMV and BMV 1a proteins and TMV p126. We show here that these domains have homology with portions of the Sindbis proteins nsP1 and nsP2, respectively. These results strengthen the view that the four viruses share mechanistic similarities in their replication strategies and may be evolutionarily related. These results also suggest that either the AlMV 1a, BMV 1a, and TMV p126 proteins are multifunctional or Sindbis proteins nsP1 and nsP2 function together as subunits in a single complex.
D000595:Amino Acid Sequence; D005075:Biological Evolution; D005814:Genes, Viral; D009029:Mosaic Viruses / Q000032:analysis* / Q000235:genetics; D012367:RNA, Viral / Q000235:genetics; D012845:Sindbis Virus / Q000032:analysis* / Q000235:genetics; D014027:Tobacco Mosaic Virus / Q000032:analysis / Q000235:genetics; D014764:Viral Proteins
D012367:RNA, Viral; D014764:Viral Proteins