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Structural basis of Eco1-mediated cohesin acetylation

DOI: 10.1038/srep44313 DOI Help

Authors: William C. H. Chao (The Francis Crick Institute) , Benjamin O. Wade (The Francis Crick Institute) , Céline Bouchoux (The Francis Crick Institute) , Andrew W. Jones (The Francis Crick Institute) , Andy G. Purkiss (The Francis Crick Institute) , Stefania Federico (The Francis Crick Institute) , Nicola O’reilly (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: Scientific Reports , VOL 7

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

Open Access Open Access

Abstract: Sister-chromatid cohesion is established by Eco1-mediated acetylation on two conserved tandem lysines in the cohesin Smc3 subunit. However, the molecular basis of Eco1 substrate recognition and acetylation in cohesion is not fully understood. Here, we discover and rationalize the substrate specificity of Eco1 using mass spectrometry coupled with in-vitro acetylation assays and crystallography. Our structures of the X. laevis Eco2 (xEco2) bound to its primary and secondary Smc3 substrates demonstrate the plasticity of the substrate-binding site, which confers substrate specificity by concerted conformational changes of the central β hairpin and the C-terminal extension.

Journal Keywords: Acetylation; Chromosomes; Enzyme mechanisms; Mass spectrometry; X-ray crystallography

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography

Added On: 29/03/2017 16:03


Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)