A novel viral RNA helicase with an independent translation enhancement activity

FEBS Lett. 2016 Apr;590(8):1187-99. doi: 10.1002/1873-3468.12145. Epub 2016 Apr 8.

Abstract

RNA helicases have not been identified among negative sense RNA viruses. In this study, it is shown that Nonstructural protein (NSs) of Groundnut bud necrosis virus (GBNV) acts as a Mg(2+) - and ATP-dependent bipolar RNA helicase. Biophysical and biochemical analysis of the deletion mutants (NΔ124 NSs, CΔ80 NSs) revealed that both the N- and C-terminal residues are required for substrate binding, oligomerization and helicase activity, but are dispensable for ATPase activity. Interestingly, NSs could enhance the translation of RNA (~ 10-fold) independent of its helicase activity. This is the first report of a RNA helicase from negative strand RNA viruses.

Keywords: Groundnut bud necrosis virus; bipolar RNA helicase; nonstructural protein; translation enhancer.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Amino Acid Sequence
  • Biophysical Phenomena
  • Mutant Proteins / isolation & purification
  • Plant Viruses / enzymology*
  • Protein Biosynthesis*
  • RNA Helicases / chemistry
  • RNA Helicases / genetics
  • RNA Helicases / metabolism*
  • RNA, Viral / metabolism
  • Sequence Deletion
  • Surface Plasmon Resonance
  • Viral Nonstructural Proteins / isolation & purification
  • Viral Nonstructural Proteins / metabolism

Substances

  • Mutant Proteins
  • RNA, Viral
  • Viral Nonstructural Proteins
  • Adenosine Triphosphatases
  • RNA Helicases

Associated data

  • GENBANK/AAB04144.1