6533b7d4fe1ef96bd126350f

RESEARCH PRODUCT

Histone H3 Lysine 4 Mono-methylation does not Require Ubiquitination of Histone H2B

Ramon SendraDaniéle MoinierMercè PamblancoPierre LucianoPierre-marie DehéAlain VerreaultVincent GéliRégine LebrunVicente Tordera

subject

Histone H3 Lysine 4UbiquitinLysineSaccharomyces cerevisiaeBiologyMethylationenvironment and public healthMolecular biologyCell biologyHistonesHistone H1Structural BiologyHistone methyltransferaseHistone H2AHistone methylationHistone H2BHistone codeHistone octamerMolecular Biology

description

The yeast Set1-complex catalyzes histone H3 lysine 4 (H3K4) methylation. Using N-terminal Edman sequencing, we determined that 50% of H3K4 is methylated and consists of roughly equal amounts of mono, di and tri-methylated H3K4. We further show that loss of either Paf1 of the Paf1 elongation complex, or ubiquitination of histone H2B, has only a modest effect on bulk histone mono-methylation at H3K4. Despite the fact that Set1 recruitment decreases in paf1delta cells, loss of Paf1 results in an increase of H3K4 mono-methylation at the 5' coding region of active genes, suggesting a Paf1-independent targeting of Set1. In contrast to Paf1 inactivation, deleting RTF1 affects H3K4 mono-methylation at the 3' coding region of active genes and results in a decrease of global H3K4 mono-methylation. Our results indicate that the requirements for mono-methylation are distinct from those for H3K4 di and tri-methylation, and point to differences among members of the Paf1 complex in the regulation of H3K4 methylation.

yearjournalcountryeditionlanguage
2005-07-07Journal of Molecular Biology
https://doi.org/10.1016/j.jmb.2005.08.059