STRUCTURE AND FUNCTION OF RECA-DNA COMPLEXES

被引：63

作者：

STASIAK, A ^{[1
]}

EGELMAN, EH ^{[1
]}

机构：

[1] UNIV MINNESOTA, SCH MED, DEPT CELL BIOL & NEUROANAT, MINNEAPOLIS, MN 55455 USA

来源：

EXPERIENTIA | 1994年 / 50卷 / 03期

关键词：

RECA; RECA-DNA COMPLEXES; HOMOLOGOUS RECOMBINATION; RAD51; PROTEIN; ELECTRON MICROSCOPY; IMAGE ANALYSIS;

D O I：

10.1007/BF01924002

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

While the E. coli RecA protein has been the most intensively studied enzyme of homologous recombination, the unusual RecA-DNA filament has stood alone until very recently. It now appears that this protein is part of a universal family that spans all of biology, and the filament that is formed by the protein on DNA is a universal structure. With RecA's role in recombination given new and greatly increased significance, we focus in this review on the energetics of the RecA-mediated strand exchange and the relation between the energetics and recombination spanning heterologous inserts.

引用

页码：192 / 203

页数：12

共 58 条

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