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The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5′-to-3′ polarity

Published online by Cambridge University Press:  01 July 2000

ANJA SEYBERT ,
ANNETTE HEGYI ,
STUART G. SIDDELL  and
JOHN ZIEBUHR
ANJA SEYBERT
Affiliation:
Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany
ANNETTE HEGYI
Affiliation:
Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany
STUART G. SIDDELL
Affiliation:
Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany
JOHN ZIEBUHR
Affiliation:
Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany

Abstract

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The human coronavirus 229E replicase gene encodes a protein, p66HEL, that contains a putative zinc finger structure linked to a putative superfamily (SF) 1 helicase. A histidine-tagged form of this protein, HEL, was expressed using baculovirus vectors in insect cells. The purified recombinant protein had in vitro ATPase activity that was strongly stimulated by poly(U), poly(dT), poly(C), and poly(dA), but not by poly(G). The recombinant protein also had both RNA and DNA duplex-unwinding activities with 5′-to-3′ polarity. The DNA helicase activity of the enzyme preferentially unwound 5′-oligopyrimidine-tailed, partial-duplex substrates and required a tail length of at least 10 nucleotides for effective unwinding. The combined data suggest that the coronaviral SF1 helicase functionally differs from the previously characterized RNA virus SF2 helicases.

Keywords

5′-to-3′ polarityhelicasenucleoside triphosphatasesuperfamily 1
Type
Research Article
Information
RNA , Volume 6 , Issue 7 , July 2000 , pp. 1056 - 1068
Copyright
2000 RNA Society