English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Molecular Basis for SMC Rod Formation and Its Dissolution upon DNA Binding

Soh, Y.-M., Bürmann, F., Shin, H.-C., Oda, T., Jin, K. S., Toseland, C. P., et al. (2015). Molecular Basis for SMC Rod Formation and Its Dissolution upon DNA Binding. MOLECULAR CELL, 57(2), 290-303. doi:10.1016/j.molcel.2014.11.023.

Item is

Files

show Files
hide Files
:
1-s2.0-S1097276514009186-main.pdf (Any fulltext), 5MB
Name:
1-s2.0-S1097276514009186-main.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
open access article
License:
-

Locators

show

Creators

show
hide
 Creators:
Soh, Young-Min1, Author
Bürmann, Frank2, Author           
Shin, Ho-Chul1, Author
Oda, Takashi1, Author
Jin, Kyeong Sik1, Author
Toseland, Christopher P.2, Author           
Kim, Cheolhee1, Author
Lee, Hansol1, Author
Kim, Soo Jin1, Author
Kong, Min-Seok1, Author
Durand-Diebold, Marie-Laure2, Author           
Kim, Yeon-Gil1, Author
Kim, Ho Min1, Author
Lee, Nam Ki1, Author
Sato, Mamoru1, Author
Oh, Byung-Ha1, Author
Gruber, Stephan2, Author           
Affiliations:
1external, ou_persistent22              
2Gruber, Stephan / Chromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565151              

Content

show
hide
Free keywords: X-RAY-SCATTERING; HINGE DOMAIN; CHROMOSOME CONDENSATION; FUNCTIONAL IMPLICATIONS; STRUCTURAL MAINTENANCE; BACILLUS-SUBTILIS; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; ATP HYDROLYSIS; COMPLEX
 Abstract: 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.

Details

show
hide
Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: MOLECULAR CELL
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 57 (2) Sequence Number: - Start / End Page: 290 - 303 Identifier: ISSN: 1097-2765