[The multifunctional RNA polymerase L protein of non-segmented negative strand RNA viruses catalyzes unique mRNA capping]

Uirusu. 2014;64(2):165-78. doi: 10.2222/jsv.64.165.
[Article in Japanese]

Abstract

Non-segmented negative strand RNA viruses belonging to the Mononegavirales order possess RNA-dependent RNA polymerase L proteins within viral particles. The L protein is a multifunctional enzyme catalyzing viral RNA synthesis and processing (i.e., mRNA capping, cap methylation, and polyadenylation). Using vesicular stomatitis virus (VSV) as a prototypic model virus, we have shown that the L protein catalyzes the unconventional mRNA capping reaction, which is strikingly different from the eukaryotic reaction. Furthermore, co-transcriptional pre-mRNA capping with the VSV L protein was found to be required for accurate stop?start transcription to synthesize full-length mRNAs in vitro and virus propagation in host cells. This article provides a review of historical and present studies leading to the elucidation of the molecular mechanism of VSV mRNA capping.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Catalysis
  • Humans
  • RNA Caps / metabolism*
  • RNA Viruses / genetics*
  • RNA, Messenger / metabolism*
  • RNA, Viral / metabolism*
  • RNA-Dependent RNA Polymerase / chemistry
  • RNA-Dependent RNA Polymerase / physiology*
  • Transcription, Genetic
  • Vesicular stomatitis Indiana virus / genetics*
  • Vesicular stomatitis Indiana virus / growth & development
  • Viral Proteins / chemistry
  • Viral Proteins / physiology*

Substances

  • RNA Caps
  • RNA, Messenger
  • RNA, Viral
  • Viral Proteins
  • L protein, vesicular stomatitis virus
  • RNA-Dependent RNA Polymerase