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dc.contributor.author Wong, Sarah J.
dc.contributor.author Gearhart, Micah D.
dc.contributor.author Taylor, Alexander B.
dc.contributor.author Nanyes, David R.
dc.contributor.author Ha, Daniel J.
dc.contributor.author Robinson, Angela K.
dc.contributor.author Artigas, Jason A.
dc.contributor.author Lee, Oliver J.
dc.contributor.author Demeler, Borries
dc.contributor.author Hart, P. John
dc.contributor.author Bardwell, Vivian J.
dc.contributor.author Kim, Chongwoo A.
dc.date.accessioned 2021-10-06T21:28:48Z
dc.date.available 2021-10-06T21:28:48Z
dc.date.issued 2016
dc.identifier.citation Wong, 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.2016.07.011 en_US
dc.identifier.uri https://hdl.handle.net/10133/6056
dc.description Accepted author manuscript en_US
dc.description.abstract KDM2B 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.language.iso en_US en_US
dc.publisher Elsevier en_US
dc.subject KDM2B
dc.subject BCORL1
dc.subject PCGF1
dc.subject Protein purification
dc.subject Analytical ultracentrifugation
dc.subject Isothermal titration calorimetry
dc.subject X-ray crystallography
dc.subject Ni2+ pull-down assay
dc.subject.lcsh Proteins--Research
dc.title KDM2B recruitment of the polycomb group complex, PRC1.1, requires cooperation between PCGF1 and BCORL1 en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution University of Texas Health Science Center at San Antonio en_US
dc.publisher.institution University of Minnesota en_US
dc.publisher.institution Midwestern University en_US
dc.publisher.institution South Texas Veterans Health Care System en_US
dc.publisher.institution University of Lethbridge en_US
dc.publisher.url https://doi.org/10.1016/j.str.2016.07.011 en_US


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