BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization

Felicia Gray, Hyo Je Cho, Shirish Shukla, Shihan He, Ashley Harris, Bohdan Boytsov, Łukasz Jaremko, Mariusz Jaremko, Borries Demeler, Elizabeth R. Lawlor, Jolanta Grembecka and Tomasz Cierpicki ()
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Felicia Gray: University of Michigan
Hyo Je Cho: University of Michigan
Shirish Shukla: University of Michigan
Shihan He: University of Michigan
Ashley Harris: Translational Oncology Program, University of Michigan
Bohdan Boytsov: University of Michigan
Łukasz Jaremko: Deutsches Zentrum fur Neurodegenerative Erkrankungen (DZNE)
Mariusz Jaremko: Max-Planck Institute of Biophysical Chemistry
Borries Demeler: The University of Texas Health Science Center at San Antonio
Elizabeth R. Lawlor: University of Michigan
Jolanta Grembecka: University of Michigan
Tomasz Cierpicki: University of Michigan

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract BMI1 is a core component of the polycomb repressive complex 1 (PRC1) and emerging data support a role of BMI1 in cancer. The central domain of BMI1 is involved in protein–protein interactions and is essential for its oncogenic activity. Here, we present the structure of BMI1 bound to the polyhomeotic protein PHC2 illustrating that the central domain of BMI1 adopts an ubiquitin-like (UBL) fold and binds PHC2 in a β-hairpin conformation. Unexpectedly, we find that the UBL domain is involved in homo-oligomerization of BMI1. We demonstrate that both the interaction of BMI1 with polyhomeotic proteins and homo-oligomerization via UBL domain are necessary for H2A ubiquitination activity of PRC1 and for clonogenic potential of U2OS cells. Here, we also emphasize need for joint application of NMR spectroscopy and X-ray crystallography to determine the overall structure of the BMI1–PHC2 complex.

Date: 2016
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DOI: 10.1038/ncomms13343

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