A novel viral RNA helicase with an independent translation enhancement activity

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 Mg2+‐ and ATP‐dependent bipolar RNA helicase. Biophysical and biochemical analysis of the deletion mutants (NΔ124 NSs,...

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Bibliographic Details
Published in:FEBS letters 2016-04, Vol.590 (8), p.1187-1199
Main Authors: Abraham, Ambily, Savithri, Handanahal S.
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Amino Acid Sequence
Biophysical Phenomena
bipolar RNA helicase
Groundnut bud necrosis virus
Mutant Proteins - isolation & purification
nonstructural protein
Plant Viruses - enzymology
Protein Biosynthesis
RNA Helicases - chemistry
RNA Helicases - genetics
RNA Helicases - metabolism
RNA, Viral - metabolism
Sequence Deletion
Surface Plasmon Resonance
translation enhancer
Viral Nonstructural Proteins - isolation & purification
Viral Nonstructural Proteins - metabolism
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Summary: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 Mg2+‐ 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. GBNV NSs—first RNA helicase of negative strand RNA viruses N‐ and C‐terminal domains—crucial for oligomerization, RNA binding, helicase activity N‐ and C‐terminal domains—dispensable for ATPase activity GBNV NSs—enhancer of translation independent of its helicase activity
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12145