KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1

Sarah J. Wong, Micah D. Gearhart, Alexander B. Taylor, David R. Nanyes, Daniel J. Ha, Angela K. Robinson, Jason A. Artigas, Oliver J. Lee, Borries Demeler, P. John Hart, Vivian J. Bardwell, Chongwoo A. Kim

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

KDM2B recruits H2A-ubiquitinating activity of a non-canonical Polycomb Repression Complex 1 (PRC1.1) to CpG islands, facilitating gene repression. We investigated the molecular basis of recruitment 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 heterodimer 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 heterodimer. The BCORL1 PUFD domain positions residues 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.

Original languageEnglish (US)
Pages (from-to)1795-1801
Number of pages7
JournalStructure
Volume24
Issue number10
DOIs
StatePublished - Oct 4 2016

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SKP Cullin F-Box Protein Ligases
CpG Islands
Brain Neoplasms
Pediatrics
Kidney
DNA
Genes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Wong, S. J., Gearhart, M. D., Taylor, A. B., Nanyes, D. R., Ha, D. J., Robinson, A. K., ... 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

KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1. / 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; Bardwell, Vivian J.; Kim, Chongwoo A.

In: Structure, Vol. 24, No. 10, 04.10.2016, p. 1795-1801.

Research output: Contribution to journalArticle

Wong, SJ, Gearhart, MD, Taylor, AB, Nanyes, DR, Ha, DJ, Robinson, AK, Artigas, JA, Lee, OJ, Demeler, B, Hart, PJ, Bardwell, VJ & Kim, CA 2016, 'KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1', Structure, vol. 24, no. 10, pp. 1795-1801. https://doi.org/10.1016/j.str.2016.07.011
Wong SJ, Gearhart MD, Taylor AB, Nanyes DR, Ha DJ, Robinson AK et al. KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1. Structure. 2016 Oct 4;24(10):1795-1801. https://doi.org/10.1016/j.str.2016.07.011
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 ; Bardwell, Vivian J. ; Kim, Chongwoo A. / KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1. In: Structure. 2016 ; Vol. 24, No. 10. pp. 1795-1801.
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abstract = "KDM2B recruits H2A-ubiquitinating activity of a non-canonical Polycomb Repression Complex 1 (PRC1.1) to CpG islands, facilitating gene repression. We investigated the molecular basis of recruitment 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 heterodimer 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 heterodimer. The BCORL1 PUFD domain positions residues 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.",
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