Enzyme-mediated DNA looping

被引:88
作者
Halford, SE [1 ]
Welsh, AJ [1 ]
Szczelkun, MD [1 ]
机构
[1] Univ Bristol, Sch Med Sci, Dept Biochem, Bristol BS8 1TD, Avon, England
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 2004年 / 33卷
关键词
restriction endonuclease; DNA structure; DNA-protein interaction; protein-protein interaction; molecular motor;
D O I
10.1146/annurev.biophys.33.110502.132711
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
Most reactions on DNA are carried out by multimeric protein complexes that interact with two or more sites in the DNA and thus loop out the DNA between the sites. The enzymes that catalyze these reactions usually have no activity until they interact with both sites. This review examines the mechanisms for the assembly of protein complexes spanning two DNA sites and the resultant triggering of enzyme activity. There are two main routes for bringing together distant DNA sites in an enzyme complex: either the proteins bind concurrently to both sites and capture the intervening DNA in a loop, or they translocate the DNA between one site and another into an expanding loop, by an energy-dependent translocation mechanism. Both capture and translocation mechanisms are discussed here, with reference to the various types of restriction endonuclease that interact with two recognition sites before cleaving DNA.
引用
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页码:1 / 24
页数:24
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