Separate molecules of West Nile virus methyltransferase can independently catalyze the N7 and 2'-O methylations of viral RNA cap

Virology. 2008 Jul 20;377(1):1-6. doi: 10.1016/j.virol.2008.04.026. Epub 2008 May 23.

Abstract

West Nile virus methyltransferase catalyzes N7 and 2'-O methylations of the viral RNA cap (GpppA-RNA-->m(7)GpppAm-RNA). The two methylation events are independent, as evidenced by efficient N7 methylation of GpppA-RNA-->m(7)GpppA-RNA and GpppAm-RNA-->m(7)GpppAm-RNA, and by the 2'-O methylation of GpppA-RNA-->GpppAm-RNA and m(7)GpppA-RNA-->m(7)GpppAm-RNA. However, the 2'-O methylation activity prefers substrate m(7)GpppA-RNA to GpppA-RNA, thereby determining the dominant methylation pathway as GpppA-RNA-->m(7)GpppA-RNA-->m(7)GpppAm-RNA. Mutant enzymes with different methylation defects can trans complement one another in vitro. Furthermore, sequential treatment of GpppA-RNA with distinct methyltransferase mutants generates fully methylated m(7)GpppAm-RNA, demonstrating that separate molecules of the enzyme can independently catalyze the two cap methylations in vitro.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Genes, Viral
  • Genetic Complementation Test
  • Kinetics
  • Methylation
  • Methyltransferases / chemistry
  • Methyltransferases / genetics
  • Methyltransferases / metabolism*
  • Models, Molecular
  • Mutation
  • RNA Cap Analogs / metabolism
  • RNA Caps / chemistry
  • RNA Caps / genetics
  • RNA Caps / metabolism*
  • RNA, Viral / chemistry
  • RNA, Viral / genetics
  • RNA, Viral / metabolism*
  • Substrate Specificity
  • West Nile virus / enzymology
  • West Nile virus / genetics
  • West Nile virus / metabolism*

Substances

  • RNA Cap Analogs
  • RNA Caps
  • RNA, Viral
  • m7GpppA
  • Methyltransferases