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

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.

Authors:
; ; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE; National Institutes of Health (NIH)
Contributing Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
OSTI Identifier:
1313242
Alternate Identifier(s):
OSTI ID: 1328788
Grant/Contract Number:  
AC02–06CH11357
Resource Type:
Published Article
Journal Name:
Structure
Additional Journal Information:
Journal Name: Structure Journal Volume: 24 Journal Issue: 10; Journal ID: ISSN 0969-2126
Publisher:
Elsevier
Country of Publication:
United Kingdom
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

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., and Kim, Chongwoo A. KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1. United Kingdom: N. p., 2016. Web. doi: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. United Kingdom. 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., and Kim, Chongwoo A. Sat . "KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1". United Kingdom. https://doi.org/10.1016/j.str.2016.07.011.
@article{osti_1313242,
title = {KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires Cooperation between PCGF1 and BCORL1},
author = {Wong, Sarah J. and Gearhart, Micah D. and Taylor, Alexander B. and Nanyes, David R. and Ha, Daniel J. and Robinson, Angela K. and Artigas, Jason A. and Lee, Oliver J. and Demeler, Borries and Hart, P. John and Bardwell, Vivian J. and Kim, Chongwoo A.},
abstractNote = {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.},
doi = {10.1016/j.str.2016.07.011},
journal = {Structure},
number = 10,
volume = 24,
place = {United Kingdom},
year = {Sat Oct 01 00:00:00 EDT 2016},
month = {Sat Oct 01 00:00:00 EDT 2016}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1016/j.str.2016.07.011

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Works referencing / citing this record:

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KDM2B in polycomb repressive complex 1.1 functions as a tumor suppressor in the initiation of T-cell leukemogenesis
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