Molecular basis for SMC rod formation and its dissolution upon DNA binding.

Détails

ID Serval
serval:BIB_177609129EF8
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Molecular basis for SMC rod formation and its dissolution upon DNA binding.
Périodique
Molecular Cell
Auteur⸱e⸱s
Soh Y.M., Bürmann F., Shin H.C., Oda T., Jin K.S., Toseland C.P., Kim C., Lee H., Kim S.J., Kong M.S., Durand-Diebold M.L., Kim Y.G., Kim H.M., Lee N.K., Sato M., Oh B.H., Gruber S.
ISSN
1097-4164 (Electronic)
ISSN-L
1097-2765
Statut éditorial
Publié
Date de publication
2015
Peer-reviewed
Oui
Volume
57
Numéro
2
Pages
290-303
Langue
anglais
Résumé
SMC condensin complexes are central modulators of chromosome superstructure in all branches of life. Their SMC subunits form a long intramolecular coiled coil, which connects a constitutive "hinge" dimerization domain with an ATP-regulated "head" dimerization module. Here, we address the structural arrangement of the long coiled coils in SMC complexes. We unequivocally show that prokaryotic Smc-ScpAB, eukaryotic condensin, and possibly also cohesin form rod-like structures, with their coiled coils being closely juxtaposed and accurately anchored to the hinge. Upon ATP-induced binding of DNA to the hinge, however, Smc switches to a more open configuration. Our data suggest that a long-distance structural transition is transmitted from the Smc head domains to regulate Smc-ScpAB's association with DNA. These findings uncover a conserved architectural theme in SMC complexes, provide a mechanistic basis for Smc's dynamic engagement with chromosomes, and offer a molecular explanation for defects in Cornelia de Lange syndrome.
Mots-clé
Amino Acid Sequence, Bacterial Proteins/chemistry, Bacterial Proteins/ultrastructure, Cell Cycle Proteins/chemistry, Cell Cycle Proteins/ultrastructure, Crystallography, X-Ray, DNA, Bacterial/chemistry, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Secondary, Pyrococcus furiosus
Pubmed
Web of science
Open Access
Oui
Création de la notice
17/08/2016 9:48
Dernière modification de la notice
20/08/2019 12:47
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