What is the structure of the RecA-DNA filament?

被引：32

作者：

Yu, X ^{[1
]}

VanLoock, MS ^{[1
]}

Yang, S ^{[1
]}

Reese, JT ^{[1
]}

Egelman, EH ^{[1
]}

机构：

[1] Univ Virginia, Hlth Sci Ctr, Dept Biochem & Mol Genet, Charlottesville, VA 22908 USA

来源：

CURRENT PROTEIN & PEPTIDE SCIENCE | 2004年 / 5卷 / 02期

关键词：

D O I：

10.2174/1389203043486883

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 bacterial RecA protein has been a model system for understanding how a protein can catalyze homologous genetic recombination. RecA-like proteins have now been characterized from many organisms, from bacteriophage to humans. Some of the RecA-like proteins, including, human RAD51, appear to function as helical filaments formed on DNA. However, we currently have high resolution Structures of inactive forms of the protein, and low resolution structures of the active complexes formed by RecA-like proteins on DNA in the presence of ATP or ATP analogs. Within a crystal of the E. coli RecA protein, a helical polymer exists, and it has been widely assumed that this polymer is quite similar to the active helical filament formed on DNA. Recent developments have suggested that this may not be the case.

引用

页码：73 / 79

页数：7

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