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

Dehé, Pierre-Marie; Pamblanco, Mercè; Luciano, Pierre; Lebrun, Régine; Moinier, Danièle; Sendra, Ramón; Verreault, Alain; Tordera, Vicente; Géli, Vincent

doi:10.1016/j.jmb.2005.08.059

Cited by 60 publications

(61 citation statements)

References 28 publications

(41 reference statements)

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“…Interestingly, Drtf1, but none of the other Paf1C mutants (Dpaf1, Dleo1, Dctr9, and Dcdc73) displayed a strong benomyl phenotype. Since Drtf1 is associated with global loss of H3K4 me1 (Ng et al 2003a;Dehe et al 2005), it confirmed that benomyl resistance may be largely due to the loss of this modification. In contrast, the Not4 ubiquitin ligase (E3) that regulates levels of the Jhd2 demethylase (Mersman et al 2009) did not impact on benomyl resistance, consistent with its requirement for H3K4 me3 (Laribee et al 2007;Mulder et al 2007); furthermore, no resistance was observed with Dccr4, which forms an alternative deadenylase complex with Not4 (Tucker et al 2001).…”

Section: Dissection Of Benomyl-resistance Pathways Identifies Dpho23mentioning

confidence: 71%

Coordination of Cell Cycle Progression and Mitotic Spindle Assembly Involves Histone H3 Lysine 4 Methylation by Set1/COMPASS

et al. 2017

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Methylation of histone H3 lysine 4 (H3K4) by Set1 complex/COMPASS is a hallmark of eukaryotic chromatin, but it remains poorly understood how this post-translational modification contributes to the regulation of biological processes like the cell cycle. Here, we report a H3K4 methylation-dependent pathway in Saccharomyces cerevisiae that governs toxicity toward benomyl, a microtubule destabilizing drug. Benomyl-sensitive growth of wild-type cells required mono-and dimethylation of H3K4 and Pho23, a PHD-containing subunit of the Rpd3L complex. Dset1 and Dpho23 deletions suppressed defects associated with ipl1-2 aurora kinase mutant, an integral component of the spindle assembly checkpoint during mitosis. Benomyl resistance of Dset1 strains was accompanied by deregulation of all four tubulin genes and the phenotype was suppressed by tub2-423 and Dtub3 mutations, establishing a genetic link between H3K4 methylation and microtubule function. Most interestingly, sine wave fitting and clustering of transcript abundance time series in synchronized cells revealed a requirement for Set1 for proper cell-cycle-dependent gene expression and Dset1 cells displayed delayed entry into S phase. Disruption of G1/S regulation in Dmbp1 and Dswi4 transcription factor mutants duplicated both benomyl resistance and suppression of ipl1-2 as was observed with Dset1. Taken together our results support a role for H3K4 methylation in the coordination of cell-cycle progression and proper assembly of the mitotic spindle during mitosis.

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Section: Dissection Of Benomyl-resistance Pathways Identifies Dpho23mentioning

confidence: 71%

Coordination of Cell Cycle Progression and Mitotic Spindle Assembly Involves Histone H3 Lysine 4 Methylation by Set1/COMPASS

et al. 2017

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“…Although this result does not distinguish whether Swd2 and Set1 bind in sequence or together, it argues H3K4 monomethylation is not sufficient and that Set1 is important for Swd2 cross-linking. Dehé et al (59) did not observe a similar loss of Set1 binding in the rad6⌬ strain, but Vitaliano-Prunier et al (60) reported that deletion of the Rad6 partner Bre1 partially reduced Swd2 recruitment without disrupting the association between Swd2 and Set1.…”

Section: Set1 Deletion Bypasses Requirement For Swd2-thementioning

confidence: 97%

Yeast Swd2 Is Essential Because of Antagonism between Set1 Histone Methyltransferase Complex and APT (Associated with Pta1) Termination Factor

Soares¹,

Buratowski

2012

Journal of Biological Chemistry

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“…In the budding yeast, Saccharomyces cerevisiae, all mono-, di-, and trimethylation of H3K4 is catalyzed by the Set1 enzyme, and the enzymatic activity of Set1 is modulated through a multi-subunit protein complex known as the Complex of Proteins Associated with Set1 (COMPASS) (Miller et al 2001;Roguev et al 2001;Nagy et al 2002;Dehe et al 2005). COMPASS is evolutionarily conserved, with functional orthologs of Set1 acting as major H3K4 histone methyltransferases (HMTs) in metazoans (Lee and Skalnik 2005;Lee et al 2007;Simonet et al 2007).…”

mentioning

confidence: 99%

dSet1 Is the Main H3K4 Di- and Tri-Methyltransferase ThroughoutDrosophilaDevelopment

Hallson

Hollebakken²,

Li³

et al. 2012

Genetics

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In eukaryotes, the post-translational addition of methyl groups to histone H3 lysine 4 (H3K4) plays key roles in maintenance and establishment of appropriate gene expression patterns and chromatin states. We report here that an essential locus within chromosome 3L centric heterochromatin encodes the previously uncharacterized Drosophila melanogaster ortholog (dSet1, CG40351) of the Set1 H3K4 histone methyltransferase (HMT). Our results suggest that dSet1 acts as a "global" or general H3K4 diand trimethyl HMT in Drosophila. Levels of H3K4 di-and trimethylation are significantly reduced in dSet1 mutants during late larval and post-larval stages, but not in animals carrying mutations in genes encoding other well-characterized H3K4 HMTs such as trr, trx, and ash1. The latter results suggest that Trr, Trx, and Ash1 may play more specific roles in regulating key cellular targets and pathways and/ or act as global H3K4 HMTs earlier in development. In yeast and mammalian cells, the HMT activity of Set1 proteins is mediated through an evolutionarily conserved protein complex known as Complex of Proteins Associated with Set1 (COMPASS). We present biochemical evidence that dSet1 interacts with members of a putative Drosophila COMPASS complex and genetic evidence that these members are functionally required for H3K4 methylation. Taken together, our results suggest that dSet1 is responsible for the bulk of H3K4 di-and trimethylation throughout Drosophila development, thus providing a model system for better understanding the requirements for and functions of these modifications in metazoans.

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

Cited by 60 publications

References 28 publications

Coordination of Cell Cycle Progression and Mitotic Spindle Assembly Involves Histone H3 Lysine 4 Methylation by Set1/COMPASS

Coordination of Cell Cycle Progression and Mitotic Spindle Assembly Involves Histone H3 Lysine 4 Methylation by Set1/COMPASS

Yeast Swd2 Is Essential Because of Antagonism between Set1 Histone Methyltransferase Complex and APT (Associated with Pta1) Termination Factor

dSet1 Is the Main H3K4 Di- and Tri-Methyltransferase ThroughoutDrosophilaDevelopment

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