SMC condensin entraps chromosomal DNA by an ATP hydrolysis dependent loading mechanism in Bacillus subtilis.

Détails

ID Serval
serval:BIB_F252E28CF587
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
SMC condensin entraps chromosomal DNA by an ATP hydrolysis dependent loading mechanism in Bacillus subtilis.
Périodique
Elife
Auteur(s)
Wilhelm L., Bürmann F., Minnen A., Shin H.C., Toseland C.P., Oh B.H., Gruber S.
ISSN
2050-084X (Electronic)
ISSN-L
2050-084X
Statut éditorial
Publié
Date de publication
2015
Peer-reviewed
Oui
Volume
4
Pages
e06659
Langue
anglais
Résumé
Smc-ScpAB forms elongated, annular structures that promote chromosome segregation, presumably by compacting and resolving sister DNA molecules. The mechanistic basis for its action, however, is only poorly understood. Here, we have established a physical assay to determine whether the binding of condensin to native chromosomes in Bacillus subtilis involves entrapment of DNA by the Smc-ScpAB ring. To do so, we have chemically cross-linked the three ring interfaces in Smc-ScpAB and thereafter isolated intact chromosomes under protein denaturing conditions. Exclusively species of Smc-ScpA, which were previously cross-linked into covalent rings, remained associated with chromosomal DNA. DNA entrapment is abolished by mutations that interfere with the Smc ATPase cycle and strongly reduced when the recruitment factor ParB is deleted, implying that most Smc-ScpAB is loaded onto the chromosome at parS sites near the replication origin. We furthermore report a physical interaction between native Smc-ScpAB and chromosomal DNA fragments.
Mots-clé
Adenosine Triphosphatases/metabolism, Adenosine Triphosphate/biosynthesis, Bacillus subtilis, Bacterial Proteins/metabolism, Cell Cycle Proteins/metabolism, Chromosomes, Bacterial/genetics, DNA, Bacterial/metabolism, DNA-Binding Proteins/metabolism, Hydrolysis, Multiprotein Complexes/metabolism
Pubmed
Web of science
Création de la notice
17/08/2016 10:48
Dernière modification de la notice
03/03/2018 22:40
Données d'usage