Structure and function of RecA-DNA complexes.

Details

Serval ID
serval:BIB_E942227B83F4
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Institution
Title
Structure and function of RecA-DNA complexes.
Journal
Experientia
Author(s)
Stasiak A., Egelman E.H.
ISSN
0014-4754[print], 0014-4754[linking]
Publication state
Published
Issued date
03/1994
Volume
50
Number
3
Pages
192-203
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Review
Publication Status: ppublish
Abstract
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.
Keywords
Adenosine Triphosphate/metabolism, DNA/chemistry, DNA, Single-Stranded/chemistry, Deoxyribonucleoproteins/chemistry, Deoxyribonucleoproteins/ultrastructure, Models, Molecular, Rec A Recombinases/chemistry, Rec A Recombinases/genetics, Recombination, Genetic
Pubmed
Web of science
Create date
24/01/2008 10:36
Last modification date
20/08/2019 16:11
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