| Abstrakt: |
Monoubiquitination of histone H2B (to H2Bub1) is required for downstream events including histone H3 methylation, transcription, and mRNA export. The mechanisms and players regulating these events have not yet been completely delineated. Here, we show that the conserved Ran‐binding protein Mog1 is required to sustain normal levels of H2Bub1 and H3K4me3 in Saccharomyces cerevisiae. Mog1 is needed for gene body recruitment of Rad6, Bre1, and Rtf1 that are involved in H2B ubiquitination and genetically interacts with these factors. We provide evidence that the absence of MOG1 impacts on cellular processes such as transcription, DNA replication, and mRNA export, which are linked to H2Bub1. Importantly, the mRNA export defect in mog1Δ strains is exacerbated by the absence of factors that decrease H2Bub1 levels. Consistent with a role in sustaining H2Bub and H3K4me3 levels, Mog1 co‐precipitates with components that participate in these modifications such as Bre1, Rtf1, and the COMPASS‐associated factors Shg1 and Sdc1. These results reveal a novel role for Mog1 in H2B ubiquitination, transcription, and mRNA biogenesis. Synopsis: The conserved Mog1 protein is important for H2Bub1, H3K4me3, transcription, and mRNA export. This novel role is distinct from its known ability to bind Ran‐GTP during protein transport. Mog1 is required to sustain normal levels of H2Bub1 and H3K4me3 and co‐precipitates with components that participate in these modifications in Saccharomyces cerevisiae.The absence of MOG1 impacts on cellular processes linked to H2Bub1, such as transcription and mRNA export.Mog1 binding to Ran is not required for its role in epigenetic modifications. The conserved Mog1 protein is important for H2Bub1, H3K4me3, transcription, and mRNA export. This novel role is distinct from its known ability to bind Ran‐GTP during protein transport. [ABSTRACT FROM AUTHOR] |
Plný text