AustralieFrV1, Main, Exploration, bibRecord, 000F16

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

Identifieur interne : 000F16 ( Main/Exploration ); précédent : 000F15; suivant : 000F17

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

Auteurs : Traude H. Beilharz [Australie] ; Paul F. Harrison [Australie] ; Douglas Maya Miles [France] ; Michael Ming See [Australie] ; Uyen Minh Merry Le [Australie] ; Ming Kalanon [Australie] ; Melissa Jane Curtis [Australie] ; Qambar Hasan [Australie] ; Julie Saksouk [France] ; Thanasis Margaritis [Pays-Bas] ; Frank Holstege [Pays-Bas] ; Vincent Geli [France] ; Bernhard Dichtl [Australie]

Source :

Genetics [ 1943-2631 ] ; 2017.

RBID : pubmed:28049706

Descripteurs français

English descriptors

KwdEn :
- Chromatin (metabolism), DNA-Binding Proteins (metabolism), Histone-Lysine N-Methyltransferase (genetics), Histone-Lysine N-Methyltransferase (metabolism), Histones (genetics), Histones (metabolism), Lysine (metabolism), M Phase Cell Cycle Checkpoints (physiology), Methylation, Mitosis (physiology), Protein Processing, Post-Translational, Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Spindle Apparatus (metabolism), Transcription Factors (metabolism), Ubiquitination.
MESH :
- chemical , genetics : Histone-Lysine N-Methyltransferase, Histones, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Chromatin, DNA-Binding Proteins, Histone-Lysine N-Methyltransferase, Histones, Lysine, Saccharomyces cerevisiae Proteins, Transcription Factors.
- cytology : Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae, Spindle Apparatus.
- physiology : M Phase Cell Cycle Checkpoints, Mitosis.
- Methylation, Protein Processing, Post-Translational, Ubiquitination.

Abstract

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. Δset1 and Δpho23 deletions suppressed defects associated with ipl1-2 aurora kinase mutant, an integral component of the spindle assembly checkpoint during mitosis. Benomyl resistance of Δset1 strains was accompanied by deregulation of all four tubulin genes and the phenotype was suppressed by tub2-423 and Δtub3 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 Δset1 cells displayed delayed entry into S phase. Disruption of G1/S regulation in Δmbp1 and Δswi4 transcription factor mutants duplicated both benomyl resistance and suppression of ipl1-2 as was observed with Δset1 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.

DOI: 10.1534/genetics.116.194852
PubMed: 28049706

Affiliations:

Le document en format XML

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<author><name sortKey="Curtis, Melissa Jane" sort="Curtis, Melissa Jane" uniqKey="Curtis M" first="Melissa Jane" last="Curtis">Melissa Jane Curtis</name>
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<country xml:lang="fr">Australie</country>
<wicri:regionArea>Development and Stem Cells Program, Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria 3800</wicri:regionArea>
<wicri:noRegion>Victoria 3800</wicri:noRegion>
</affiliation>
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<author><name sortKey="Hasan, Qambar" sort="Hasan, Qambar" uniqKey="Hasan Q" first="Qambar" last="Hasan">Qambar Hasan</name>
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<country xml:lang="fr">Australie</country>
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<wicri:noRegion>Victoria 3125</wicri:noRegion>
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<author><name sortKey="Saksouk, Julie" sort="Saksouk, Julie" uniqKey="Saksouk J" first="Julie" last="Saksouk">Julie Saksouk</name>
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<author><name sortKey="Margaritis, Thanasis" sort="Margaritis, Thanasis" uniqKey="Margaritis T" first="Thanasis" last="Margaritis">Thanasis Margaritis</name>
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<wicri:regionArea>Molecular Cancer Research, University Medical Center Utrecht-Princess Máxima Center for Pediatric Oncology, 3584 Utrecht</wicri:regionArea>
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<author><name sortKey="Holstege, Frank" sort="Holstege, Frank" uniqKey="Holstege F" first="Frank" last="Holstege">Frank Holstege</name>
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<country xml:lang="fr">Pays-Bas</country>
<wicri:regionArea>Molecular Cancer Research, University Medical Center Utrecht-Princess Máxima Center for Pediatric Oncology, 3584 Utrecht</wicri:regionArea>
<placeName><settlement type="city">Utrecht</settlement>
<region nuts="2" type="province">Utrecht (province)</region>
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<author><name sortKey="Geli, Vincent" sort="Geli, Vincent" uniqKey="Geli V" first="Vincent" last="Geli">Vincent Geli</name>
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<country xml:lang="fr">France</country>
<wicri:regionArea>Marseille Cancer Research Center, U1068 Inserm, UMR7258 CNRS, Aix Marseille University, Institut Paoli-Calmettes, F-13009 Marseille</wicri:regionArea>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatin (metabolism)</term>
<term>DNA-Binding Proteins (metabolism)</term>
<term>Histone-Lysine N-Methyltransferase (genetics)</term>
<term>Histone-Lysine N-Methyltransferase (metabolism)</term>
<term>Histones (genetics)</term>
<term>Histones (metabolism)</term>
<term>Lysine (metabolism)</term>
<term>M Phase Cell Cycle Checkpoints (physiology)</term>
<term>Methylation</term>
<term>Mitosis (physiology)</term>
<term>Protein Processing, Post-Translational</term>
<term>Saccharomyces cerevisiae (cytology)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Spindle Apparatus (metabolism)</term>
<term>Transcription Factors (metabolism)</term>
<term>Ubiquitination</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Appareil du fuseau (métabolisme)</term>
<term>Chromatine (métabolisme)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Histone (génétique)</term>
<term>Histone (métabolisme)</term>
<term>Histone-lysine N-methyltransferase (génétique)</term>
<term>Histone-lysine N-methyltransferase (métabolisme)</term>
<term>Lysine (métabolisme)</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Mitose (physiologie)</term>
<term>Méthylation</term>
<term>Points de contrôle de la phase M du cycle cellulaire (physiologie)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de liaison à l'ADN (métabolisme)</term>
<term>Saccharomyces cerevisiae (cytologie)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Ubiquitinylation</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Histone-Lysine N-Methyltransferase</term>
<term>Histones</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chromatin</term>
<term>DNA-Binding Proteins</term>
<term>Histone-Lysine N-Methyltransferase</term>
<term>Histones</term>
<term>Lysine</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Histone</term>
<term>Histone-lysine N-methyltransferase</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
<term>Spindle Apparatus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil du fuseau</term>
<term>Chromatine</term>
<term>Facteurs de transcription</term>
<term>Histone</term>
<term>Histone-lysine N-methyltransferase</term>
<term>Lysine</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de liaison à l'ADN</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Mitose</term>
<term>Points de contrôle de la phase M du cycle cellulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>M Phase Cell Cycle Checkpoints</term>
<term>Mitosis</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Methylation</term>
<term>Protein Processing, Post-Translational</term>
<term>Ubiquitination</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Maturation post-traductionnelle des protéines</term>
<term>Méthylation</term>
<term>Ubiquitinylation</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">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. Δset1 and Δpho23 deletions suppressed defects associated with ipl1-2 aurora kinase mutant, an integral component of the spindle assembly checkpoint during mitosis. Benomyl resistance of Δset1 strains was accompanied by deregulation of all four tubulin genes and the phenotype was suppressed by tub2-423 and Δtub3 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 Δset1 cells displayed delayed entry into S phase. Disruption of G1/S regulation in Δmbp1 and Δswi4 transcription factor mutants duplicated both benomyl resistance and suppression of ipl1-2 as was observed with Δset1 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.</div>
</front>
</TEI>
<affiliations><list><country><li>Australie</li>
<li>France</li>
<li>Pays-Bas</li>
</country>
<region><li>Languedoc-Roussillon</li>
<li>Occitanie (région administrative)</li>
<li>Utrecht (province)</li>
</region>
<settlement><li>Montpellier</li>
<li>Utrecht</li>
</settlement>
</list>
<tree><country name="Australie"><noRegion><name sortKey="Beilharz, Traude H" sort="Beilharz, Traude H" uniqKey="Beilharz T" first="Traude H" last="Beilharz">Traude H. Beilharz</name>
</noRegion>
<name sortKey="Curtis, Melissa Jane" sort="Curtis, Melissa Jane" uniqKey="Curtis M" first="Melissa Jane" last="Curtis">Melissa Jane Curtis</name>
<name sortKey="Dichtl, Bernhard" sort="Dichtl, Bernhard" uniqKey="Dichtl B" first="Bernhard" last="Dichtl">Bernhard Dichtl</name>
<name sortKey="Harrison, Paul F" sort="Harrison, Paul F" uniqKey="Harrison P" first="Paul F" last="Harrison">Paul F. Harrison</name>
<name sortKey="Hasan, Qambar" sort="Hasan, Qambar" uniqKey="Hasan Q" first="Qambar" last="Hasan">Qambar Hasan</name>
<name sortKey="Kalanon, Ming" sort="Kalanon, Ming" uniqKey="Kalanon M" first="Ming" last="Kalanon">Ming Kalanon</name>
<name sortKey="Le, Uyen Minh Merry" sort="Le, Uyen Minh Merry" uniqKey="Le U" first="Uyen Minh Merry" last="Le">Uyen Minh Merry Le</name>
<name sortKey="See, Michael Ming" sort="See, Michael Ming" uniqKey="See M" first="Michael Ming" last="See">Michael Ming See</name>
</country>
<country name="France"><noRegion><name sortKey="Miles, Douglas Maya" sort="Miles, Douglas Maya" uniqKey="Miles D" first="Douglas Maya" last="Miles">Douglas Maya Miles</name>
</noRegion>
<name sortKey="Geli, Vincent" sort="Geli, Vincent" uniqKey="Geli V" first="Vincent" last="Geli">Vincent Geli</name>
<name sortKey="Saksouk, Julie" sort="Saksouk, Julie" uniqKey="Saksouk J" first="Julie" last="Saksouk">Julie Saksouk</name>
</country>
<country name="Pays-Bas"><region name="Utrecht (province)"><name sortKey="Margaritis, Thanasis" sort="Margaritis, Thanasis" uniqKey="Margaritis T" first="Thanasis" last="Margaritis">Thanasis Margaritis</name>
</region>
<name sortKey="Holstege, Frank" sort="Holstege, Frank" uniqKey="Holstege F" first="Frank" last="Holstege">Frank Holstege</name>
</country>
</tree>
</affiliations>
</record>

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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.

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