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National Academy of Sciences, Proceedings of the National Academy of Sciences, 33(118), 2021

DOI: 10.1073/pnas.2025291118

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Biochemical insights into Paf1 complex–induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination

Journal article published in 2021 by Feilong Chen ORCID, Beibei Liu, Lu Guo, Xuan Ge, Wei Feng, De-Feng Li ORCID, Hao Zhou, Jiafu Long ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Significance PAF1C is a highly conserved multiprotein complex composed of five core subunits (Paf1, Leo1, Ctr9, Cdc73, and Rtf1) and is required for Rad6/Bre1-mediated H2B monoubiquitination (H2Bub). This study involves a mechanistic analysis of the contributions of the PAF1C subunits to H2Bub. The results from an established in vitro ubiquitination assay clearly suggest that PAF1C might stimulate H2Bub through multivalent interactions with Rad6 and nucleosomal substrates to facilitate ubiquitin transfer and indicate that intact PAF1C is required to efficiently stimulate Rad6/Bre1-mediated H2Bub.