Binding and unwinding: SF3 viral helicases

被引:89
作者
Hickman, AB [1 ]
Dyda, F [1 ]
机构
[1] NIDDKD, Mol Biol Lab, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1016/j.sbi.2004.12.001
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 SF3 helicases, distinct from the more prevalent SF1 and SF2 helicases, were originally identified in the genomes of small DNA and RNA viruses. The first crystal structures of SF3 helicases have been determined, revealing a closer structural relationship to AAA+ proteins than to RecA, consistent with their participation in replication initiation. In conjunction with origin-binding domains, SF3 helicases are responsible for distorting DNA before replication forks can be assembled. At these forks, the SF3 helicases act as replicative helicases. The simian virus 40 SF3 helicase forms a hexameric ring, anticipated to be characteristic of the entire superfamily.
引用
收藏
页码:77 / 85
页数:9
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