KDM2B recruitment of the polycomb group complex, PRC1.1, requires cooperation between PCGF1 and BCORL1

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dc.contributor.authorWong, Sarah J.
dc.contributor.authorGearhart, Micah D.
dc.contributor.authorTaylor, Alexander B.
dc.contributor.authorNanyes, David R.
dc.contributor.authorHa, Daniel J.
dc.contributor.authorRobinson, Angela K.
dc.contributor.authorArtigas, Jason A.
dc.contributor.authorLee, Oliver J.
dc.contributor.authorDemeler, Borries
dc.contributor.authorHart, P. John
dc.contributor.authorBardwell, Vivian J.
dc.contributor.authorKim, Chongwoo A.
dc.date.accessioned2021-10-06T21:28:48Z
dc.date.available2021-10-06T21:28:48Z
dc.date.issued2016
dc.descriptionAccepted author manuscripten_US
dc.description.abstractKDM2B recruits H2A-ubiquitinating activity of a non-canonical Polycomb Repression Complex 1 (PRC1.1) to CpG islands, facilitating gene repres sion. We investigated the molecular basis of recruit ment using in vitro assembly assays to identify minimal components, subcomplexes, and domains required for recruitment. A minimal four-component PRC1.1 complex can be assembled by combining two separately isolated subcomplexes: the DNA binding KDM2B/SKP1 heterodimer and the hetero dimer of BCORL1 and PCGF1, a core component of PRC1.1. The crystal structure of the KDM2B/ SKP1/BCORL1/PCGF1 complex illustrates the crucial role played by the PCGF1/BCORL1 hetero dimer. The BCORL1 PUFD domain positions resi dues preceding the RAWUL domain of PCGF1 to create an extended interface for interaction with KDM2B, which is unique to the PCGF1-containing PRC1.1 complex. The structure also suggests how KDM2B might simultaneously function in PRC1.1 and an SCF ubiquitin ligase complex and the possible molecular consequences of BCOR PUFD internal tandem duplications found in pediatric kidney and brain tumors.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationWong, S. J., Gearhart, M. D., Taylor, A. B., Nanyes, D. R., Ha, D. J., Robinson, A. K., Artigas, J. A., Lee, O. J., Demeler, B., Hart, P. J., Bardwell, V. J., & Kim, C. A. (2016). KDM2B recruitment of the polycomb group complex, PRC1.1, requires cooperation between PCGF1 and BCORL1. Structure, 24(10), 1795-1801. https://doi.org/10.1016/j.str.2016.07.011en_US
dc.identifier.urihttps://hdl.handle.net/10133/6056
dc.language.isoen_USen_US
dc.publisherElsevieren_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionUniversity of Texas Health Science Center at San Antonioen_US
dc.publisher.institutionUniversity of Minnesotaen_US
dc.publisher.institutionMidwestern Universityen_US
dc.publisher.institutionSouth Texas Veterans Health Care Systemen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://doi.org/10.1016/j.str.2016.07.011en_US
dc.subjectKDM2B
dc.subjectBCORL1
dc.subjectPCGF1
dc.subjectProtein purification
dc.subjectAnalytical ultracentrifugation
dc.subjectIsothermal titration calorimetry
dc.subjectX-ray crystallography
dc.subjectNi2+ pull-down assay
dc.subject.lcshProteins--Research
dc.titleKDM2B recruitment of the polycomb group complex, PRC1.1, requires cooperation between PCGF1 and BCORL1en_US
dc.typeArticleen_US
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