Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1996982 | Molecular Cell | 2012 | 13 Pages |
SummaryThe monoubiquitylation of histone H2B plays an important role in gene expression by contributing to the regulation of transcription elongation and mRNA processing and export. We explored additional cellular functions of this histone modification by investigating its localization to intergenic regions. H2B ubiquitylation is present in chromatin around origins of DNA replication in budding yeast, and as DNA is replicated its levels are maintained on daughter strands by the Bre1 ubiquitin ligase. In the absence of H2B ubiquitylation, the prereplication complex is formed and activated, but replication fork progression is slowed down and the replisome becomes unstable in the presence of hydroxyurea. H2B ubiquitylation promotes the assembly or stability of nucleosomes on newly replicated DNA, and this function is postulated to contribute to fork progression and replisome stability.
► H2Bub1 levels are maintained on newly replicated DNA during S phase ► H2Bub1 promotes efficient replication fork progression and replisome stability ► H2Bub1 regulates nucleosome assembly or stability on newly replicated DNA