6H8Q

Structural basis for Scc3-dependent cohesin recruitment to chromatin

Summary for 6H8Q

• Entry DOI: 10.2210/pdb6h8q/pdb
• Descriptor: Cohesin subunit SCC3, Sister chromatid cohesion protein 1, DNA (5'-D(P*CP*TP*TP*TP*CP*GP*TP*TP*TP*CP*CP*TP*TP*GP*AP*AP*AP*AP*A)-3'), ... (6 entities in total)
• Functional Keywords: cohesin cell proliferation scc3 dna binding, cell cycle
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 8
• Total formula weight: 312806.57

Authors

Li, Y.,Muir, K.,Panne, D. (deposition date: 2018-08-03, release date: 2018-08-29, Last modification date: 2024-01-17)

Primary citation

Li, Y.,Muir, K.,Bowler, M.W.,Metz, J.,Haering, C.H.,Panne, D.
Structural basis for Scc3-dependent cohesin recruitment to chromatin.
Elife, 7:-, 2018

PubMed 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.

PubMed: 30109982
DOI: 10.7554/eLife.38356

Experimental method

X-RAY DIFFRACTION (3.631 Å)