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Title: Structural basis for Scc3-dependent cohesin recruitment to chromatin.
Authors: Li, Y
Muir, KW
Bowler, MW
Metz, J
Haering, CH
Panne, D
First Published: 15-Aug-2018
Publisher: eLife Sciences Publications
Citation: Elife, 2018, 7
Abstract: The cohesin ring complex is required for numerous chromosomal transactions including sister chromatid cohesion, DNA damage repair and transcriptional regulation. How cohesin engages its chromatin substrate has remained an unresolved question. We show here, by determining a crystal structure of the budding yeast cohesin HEAT-repeat subunit Scc3 bound to a fragment of the Scc1 kleisin subunit and DNA, that Scc3 and Scc1 form a composite DNA interaction module. The Scc3-Scc1 subcomplex engages double-stranded DNA through a conserved, positively charged surface. We demonstrate that this conserved domain is required for DNA binding by Scc3-Scc1 in vitro, as well as for the enrichment of cohesin on chromosomes and for cell viability. These findings suggest that the Scc3-Scc1 DNA-binding interface plays a central role in the recruitment of cohesin complexes to chromosomes and therefore for cohesin to faithfully execute its functions during cell division.
DOI Link: 10.7554/eLife.38356
eISSN: 2050-084X
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2018. This is an open-access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Description: Supplementary files . Transparent reporting form DOI: . Supplementary file 1 DNA substrates DOI: . Supplementary file 2 Yeast genotypes. All strains are derivatives of W303. DOI: . Supplementary file 3 ChIP-qPCR primer sequences (5’fi3’). DOI: Data availability Diffraction data have been deposited in PDB under the accession code 6H8Q.
Appears in Collections:Published Articles, Dept. of Molecular and Cell Biology

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