The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA.

Détails

ID Serval
serval:BIB_C1CCB5C300FC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA.
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Stasiak A., Tsaneva I.R., West S.C., Benson C.J., Yu X., Egelman E.H.
ISSN
0027-8424[print], 0027-8424[linking]
Statut éditorial
Publié
Date de publication
08/1994
Volume
91
Numéro
16
Pages
7618-7622
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Résumé
The RuvB protein is induced in Escherichia coli as part of the SOS response to DNA damage. It is required for genetic recombination and the postreplication repair of DNA. In vitro, the RuvB protein promotes the branch migration of Holliday junctions and has a DNA helicase activity in reactions that require ATP hydrolysis. We have used electron microscopy, image analysis, and three-dimensional reconstruction to show that the RuvB protein, in the presence of ATP, forms a dodecamer on double-stranded DNA in which two stacked hexameric rings encircle the DNA and are oriented in opposite directions with D6 symmetry. Although helicases are ubiquitous and essential for many aspects of DNA repair, replication, and transcription, three-dimensional reconstruction of a helicase has not yet been reported, to our knowledge. The structural arrangement that is seen may be common to other helicases, such as the simian virus 40 large tumor antigen.
Mots-clé
Algorithms, Bacterial Proteins/ultrastructure, DNA Helicases/ultrastructure, DNA, Bacterial/ultrastructure, Escherichia coli/ultrastructure, Image Processing, Computer-Assisted, Microscopy, Electron, Scanning, Models, Molecular
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 11:36
Dernière modification de la notice
09/05/2019 0:47
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