Functional analysis of the conserved histidine residue of Bamboo mosaic virus capping enzyme in the activity for the formation of the covalent enzyme-m7GMP intermediate

FEBS Lett. 2012 Jul 30;586(16):2326-31. doi: 10.1016/j.febslet.2012.05.024. Epub 2012 May 26.

Abstract

The alphavirus-like mRNA capping enzyme of Bamboo mosaic virus (BaMV) exhibits an AdoMet-dependent guanylyltransferase activity by which the methyl group of AdoMet is transferred to GTP, leading to the formation of m(7)GTP, and the m(7)GMP moiety is next transferred to the 5' end of ppRNA via a covalent enzyme-m(7)GMP intermediate. The function of the conserved H68 of the BaMV capping enzyme in the intermediate formation was analyzed by mutagenesis in this study. The nature of the bond linking the enzyme and m(7)GMP was changed in the H68C mutant protein, strongly suggesting that H68 covalently binds to m(7)GMP in the intermediate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Conserved Sequence
  • Guanosine Triphosphate / chemistry
  • Histidine / chemistry*
  • Hydroxylamine / chemistry
  • Methyltransferases / chemistry*
  • Models, Biological
  • Molecular Sequence Data
  • Mosaic Viruses / metabolism*
  • Mutagenesis
  • Mutagenesis, Site-Directed
  • Peptides / chemistry
  • Plasmids / metabolism
  • Potexvirus / metabolism*
  • RNA Caps / chemistry*

Substances

  • Peptides
  • RNA Caps
  • Hydroxylamine
  • Histidine
  • Guanosine Triphosphate
  • 16S rRNA - m7G methyltransferase
  • Methyltransferases