0000000000243895

AUTHOR

Régine Lebrun

showing 2 related works from this author

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

2005

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…

Histone H3 Lysine 4UbiquitinLysineSaccharomyces cerevisiaeBiologyMethylationenvironment and public healthMolecular biologyCell biologyHistonesHistone H1Structural BiologyHistone methyltransferaseHistone H2AHistone methylationHistone H2BHistone codeHistone octamerMolecular BiologyJournal of Molecular Biology
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Protein Interactions within the Set1 Complex and Their Roles in the Regulation of Histone 3 Lysine 4 Methylation

2006

Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex (Set1C) that methylates histone 3 lysine 4 (H3K4). Here we have determined protein/protein interactions within the complex and related the substructure to function. The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes. The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer. Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc…

Saccharomyces cerevisiae ProteinsProtein subunitLysineRNA polymerase IISaccharomyces cerevisiaeMethylationenvironment and public healthBiochemistryProtein–protein interactionHistonesSerineGene Expression Regulation FungalCoding regionMolecular BiologybiologyLysineHistone-Lysine N-MethyltransferaseCell BiologyMethylationDNA-Binding ProteinsProtein SubunitsHistoneBiochemistrybiology.proteinProtein BindingTranscription FactorsJournal of Biological Chemistry
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