5w94 | pdb_00005w94
Crystal structure of Scc4 in complex with Scc2n and Ctf19n
Structural highlights
FunctionSCC2_YEAST Plays a structural role in chromatin. Involved in sister chromatid cohesion. Forms a complex with SCC4 required for the stable association of the cohesin complex with chromatin, which may act by hydrolyzing ATP from SMC1 and SMC3 heads. Also participates in DNA repair.[1] [2] Publication Abstract from PubMedThe ring-shaped cohesin complex brings together distant DNA domains to maintain, express, and segregate the genome. Establishing specific chromosomal linkages depends on cohesin recruitment to defined loci. One such locus is the budding yeast centromere, which is a paradigm for targeted cohesin loading. The kinetochore, a multiprotein complex that connects centromeres to microtubules, drives the recruitment of high levels of cohesin to link sister chromatids together. We have exploited this system to determine the mechanism of specific cohesin recruitment. We show that phosphorylation of the Ctf19 kinetochore protein by a conserved kinase, DDK, provides a binding site for the Scc2/4 cohesin loading complex, thereby directing cohesin loading to centromeres. A similar mechanism targets cohesin to chromosomes in vertebrates. These findings represent a complete molecular description of targeted cohesin loading, a phenomenon with wide-ranging importance in chromosome segregation and, in multicellular organisms, transcription regulation. The Kinetochore Receptor for the Cohesin Loading Complex.,Hinshaw SM, Makrantoni V, Harrison SC, Marston AL Cell. 2017 Sep 21;171(1):72-84.e13. doi: 10.1016/j.cell.2017.08.017. PMID:28938124[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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