Structure and function of RecA-DNA complexes.

Détails

ID Serval
serval:BIB_E942227B83F4
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Institution
Titre
Structure and function of RecA-DNA complexes.
Périodique
Experientia
Auteur⸱e⸱s
Stasiak A., Egelman E.H.
ISSN
0014-4754[print], 0014-4754[linking]
Statut éditorial
Publié
Date de publication
03/1994
Volume
50
Numéro
3
Pages
192-203
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Review
Publication Status: ppublish
Résumé
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.
Mots-clé
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
Création de la notice
24/01/2008 11:36
Dernière modification de la notice
20/08/2019 17:11
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