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

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dc.contributor.authorGray, Felicia
dc.contributor.authorCho, Hyo Je
dc.contributor.authorShukla, Shirish
dc.contributor.authorHe, Shihan
dc.contributor.authorHarris, Ashley
dc.contributor.authorBoytsov, Bohdan
dc.contributor.authorJaremko, Lukasz
dc.contributor.authorJaremko, Mariusz
dc.contributor.authorDemeler, Borries
dc.contributor.authorLawlor, Elizabeth R.
dc.contributor.authorGrembecka, Jolanta
dc.contributor.authorCierpicki, Tomasz
dc.date.accessioned2021-07-23T23:08:03Z
dc.date.available2021-07-23T23:08:03Z
dc.date.issued2016
dc.descriptionOpen access article. Creative Commons Attribution 4.0 International LIcense (CC BY 4.0) appliesen_US
dc.description.abstractBMI1 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.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationGray, F., Cho, H. J., Shukla, S., He, S., Harris, A., Boytsov, B., Jaremko, L., Jaremko, M., Demeler, B., Lawlor, E. R., Grembecka, J., & Cierpicki, T. (2016). BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization. Nature Communications, 7, Article 13343. https://doi.org/10.1038/ncomms13343en_US
dc.identifier.urihttps://hdl.handle.net/10133/5969
dc.language.isoen_USen_US
dc.publisherNature Publishingen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionUniversity of Michiganen_US
dc.publisher.institutionMax-Planck Institute of Biophysical Chemistryen_US
dc.publisher.institutionUniversity of Texas Health Science Center at San Antonioen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://doi.org/10.1038/ncomms13343en_US
dc.subjectStructural biologyen_US
dc.subjectStructure determinationen_US
dc.subjectBMI1
dc.subject.lcshCancer
dc.subject.lcshOligomerization
dc.titleBMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerizationen_US
dc.typeArticleen_US
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