Structural Basis of Eco1-Mediated Cohesin Acetylation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

William C. H. Chao, Benjamin O. Wade, Céline Bouchoux, Andrew W. Jones, Andrew G. Purkiss, Stefania Federico, Nicola O’Reilly, Ambrosius P. Snijders, Frank Uhlmann, Martin R. Singleton

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. More... »

PAGES

44313

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep44313

DOI

http://dx.doi.org/10.1038/srep44313

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1084132206

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28290497


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