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

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Date
2016
Authors
Wong, Sarah J.
Gearhart, Micah D.
Taylor, Alexander B.
Nanyes, David R.
Ha, Daniel J.
Robinson, Angela K.
Artigas, Jason A.
Lee, Oliver J.
Demeler, Borries
Hart, P. John
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
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.
Description
Accepted author manuscript
Keywords
KDM2B , BCORL1 , PCGF1 , Protein purification , Analytical ultracentrifugation , Isothermal titration calorimetry , X-ray crystallography , Ni2+ pull-down assay
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
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