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Structure of the cohesin loader Scc2

DOI: 10.1038/ncomms13952 DOI Help

Authors: William C. H. Chao (The Francis Crick Institute) , Yasuto Murayama (The Francis Crick Institute) , Sofía Muñoz (The Francis Crick Institute) , Andrew W. Jones (The Francis Crick Institute) , Benjamin O. Wade (The Francis Crick Institute) , Andrew G. Purkiss (The Francis Crick Institute) , Xiao-Wen Hu (The Francis Crick Institute) , Aaron Borg (The Francis Crick Institute) , Ambrosius P. Snijders (The Francis Crick Institute) , Frank Uhlmann (The Francis Crick Institute) , Martin R. Singleton (The Francis Crick Institute)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 8

State: Published (Approved)
Published: January 2017
Diamond Proposal Number(s): 13775

Open Access Open Access

Abstract: The functions of cohesin are central to genome integrity, chromosome organization and transcription regulation through its prevention of premature sister-chromatid separation and the formation of DNA loops. The loading of cohesin onto chromatin depends on the Scc2–Scc4 complex; however, little is known about how it stimulates the cohesion-loading activity. Here we determine the large ‘hook’ structure of Scc2 responsible for catalysing cohesin loading. We identify key Scc2 surfaces that are crucial for cohesin loading in vivo. With the aid of previously determined structures and homology modelling, we derive a pseudo-atomic structure of the full-length Scc2–Scc4 complex. Finally, using recombinantly purified Scc2–Scc4 and cohesin, we performed crosslinking mass spectrometry and interaction assays that suggest Scc2–Scc4 uses its modular structure to make multiple contacts with cohesin.

Journal Keywords: Chromosomes; DNA

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 30/03/2017 15:32


Discipline Tags:

Genetics Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)