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

被引：114

作者：

Seybert, A ^{[1
]}

Hegyi, A ^{[1
]}

Siddell, SG ^{[1
]}

Ziebuhr, J ^{[1
]}

机构：

[1] Univ Wurzburg, Inst Virol & Immunol, D-97078 Wurzburg, Germany

来源：

RNA | 2000年 / 6卷 / 07期

关键词：

5 '-to-3 ' polarity; helicase; nucleoside triphosphatase; superfamily; 1;

D O I：

10.1017/S1355838200000728

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The human coronavirus 229E replicase gene encodes a protein, p66(HEL), 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.

引用

页码：1056 / 1068

页数：13