Structure and function of the N-terminal domain of the vesicular stomatitis virus RNA polymerase

Academic Article

Abstract

  • Viruses have various mechanisms to duplicate their genomes and produce virus-specific mRNAs. Negative-strand RNA viruses encode their own polymerases to perform each of these processes. For the nonsegmented negative-strand RNA viruses, the polymerase is comprised of the large polymerase subunit (L) and the phosphoprotein (P). L proteins from members of the Rhabdoviridae, Paramyxoviridae, and Filoviridae share sequence and predicted secondary structure homology. Here, we present the structure of the N-terminal domain (conserved region I) of the L protein from a rhabdovirus, vesicular stomatitis virus, at 1.8-Å resolution. The strictly and strongly conserved residues in this domain cluster in a single area of the protein. Serial mutation of these residues shows that many of the amino acids are essential for viral transcription but not for mRNA capping. Three-dimensional alignments show that this domain shares structural homology with polymerases from other viral families, including segmented negative-strand RNA and double-stranded RNA (dsRNA) viruses.
  • Authors

    Published In

    Digital Object Identifier (doi)

    Author List

  • Qiu S; Ogino M; Luo M; Ogino T; Green TJ
  • Start Page

  • 715
  • End Page

  • 724
  • Volume

  • 90
  • Issue

  • 2