The Set1 N-terminal domain and Swd2 interact with RNA polymerase II CTD to recruit COMPASS

Hyun Jin Bae, Marion Dubarry, Jongcheol Jeon, Luis M. Soares, Catherine Dargemont, Jaehoon Kim, Vincent Geli () and Stephen Buratowski ()
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Hyun Jin Bae: Harvard Medical School
Marion Dubarry: UMR7258 CNRS, Aix Marseille University (AMU), Institut Paoli-Calmettes. Equipe labellisée Ligue contre le cancer
Jongcheol Jeon: Harvard Medical School
Luis M. Soares: Harvard Medical School
Catherine Dargemont: UMR 9002 CNRS
Jaehoon Kim: Korea Advanced Institute of Science and Technology
Vincent Geli: UMR7258 CNRS, Aix Marseille University (AMU), Institut Paoli-Calmettes. Equipe labellisée Ligue contre le cancer
Stephen Buratowski: Harvard Medical School

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Methylation of histone H3 lysine 4 (H3K4) by Set1/COMPASS occurs co-transcriptionally, and is important for gene regulation. Set1/COMPASS associates with the RNA polymerase II C-terminal domain (CTD) to establish proper levels and distribution of H3K4 methylations. However, details of CTD association remain unclear. Here we report that the Set1 N-terminal region and the COMPASS subunit Swd2, which interact with each other, are both needed for efficient CTD binding in Saccharomyces cerevisiae. Moreover, a single point mutation in Swd2 that affects its interaction with Set1 also impairs COMPASS recruitment to chromatin and H3K4 methylation. A CTD interaction domain (CID) from the protein Nrd1 can partially substitute for the Set1 N-terminal region to restore CTD interactions and histone methylation. However, even when Set1/COMPASS is recruited via the Nrd1 CID, histone H2B ubiquitylation is still required for efficient H3K4 methylation, indicating that H2Bub acts after the initial recruitment of COMPASS to chromatin.

Date: 2020
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DOI: 10.1038/s41467-020-16082-2

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