Structural Basis of Eco1-Mediated Cohesin Acetylation

被引：0
作者：
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
机构：
[1] Structural Biology of Chromosome Segregation Laboratory,
[2] The Francis Crick Institute,undefined
[3] Chromosome Segregation Laboratory,undefined
[4] The Francis Crick Institute,undefined
[5] Protein Analysis and Proteomics Platform,undefined
[6] The Francis Crick Institute,undefined
[7] Structural Biology Platform,undefined
[8] The Francis Crick Institute,undefined
[9] Peptide Chemistry Laboratory,undefined
[10] The Francis Crick Institute,undefined
来源：
Scientific Reports | / 7卷
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摘要：
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.
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