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. 1997 Oct;71(10):7220–7226. doi: 10.1128/jvi.71.10.7220-7226.1997

Bluetongue virus VP6 protein binds ATP and exhibits an RNA-dependent ATPase function and a helicase activity that catalyze the unwinding of double-stranded RNA substrates.

N Stäuber 1, J Martinez-Costas 1, G Sutton 1, K Monastyrskaya 1, P Roy 1
PMCID: PMC192062  PMID: 9311795

Abstract

RNA-dependent ATPase and helicase activities have been identified associated with the purified VP6 protein of bluetongue virus, a member of the Orbivirus genus of double-stranded RNA (dsRNA; Reoviridae family) viruses. In addition, the protein has an ATP binding activity. RNA unwinding of duplexes occurred with both 3' and 5' overhang templates, as well as with blunt-ended dsRNA, an activity not previously identified in other viral helicases. Although little sequence similarity to other helicases was detected, certain similarities to motifs commonly attributed to such proteins were identified.

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Selected References

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