STRUCTURE AND FUNCTION OF RECA-DNA COMPLEXES

Citation
A. Stasiak et Eh. Egelman, STRUCTURE AND FUNCTION OF RECA-DNA COMPLEXES, Experientia, 50(3), 1994, pp. 192-203
Citations number
58
Categorie Soggetti
Multidisciplinary Sciences
Journal title
ISSN journal
00144754
Volume
50
Issue
3
Year of publication
1994
Pages
192 - 203
Database
ISI
SICI code
0014-4754(1994)50:3<192:SAFORC>2.0.ZU;2-5
Abstract
While the E. coli RecA protein has been the most intensively studied e nzyme of homologous recombination, the unusual RecA-DNA filament has s tood alone until very recently. It now appears that this protein is pa rt of a universal family that spans all of biology, and the filament t hat is formed by the protein on DNA is a universal structure. With Rec A's role in recombination given new and greatly increased significance , we focus in this review on the energetics of the RecA-mediated stran d exchange and the relation between the energetics and recombination s panning heterologous inserts.