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  1. Article ; Online: Histone phosphorylation: a chromatin modification involved in diverse nuclear events.

    Rossetto, Dorine / Avvakumov, Nikita / Côté, Jacques

    Epigenetics

    2012  Volume 7, Issue 10, Page(s) 1098–1108

    Abstract: Histone posttranslational modifications are key components of diverse processes that modulate chromatin structure. These marks function as signals during various chromatin-based events, and act as platforms for recruitment, assembly or retention of ... ...

    Abstract Histone posttranslational modifications are key components of diverse processes that modulate chromatin structure. These marks function as signals during various chromatin-based events, and act as platforms for recruitment, assembly or retention of chromatin-associated factors. The best-known function of histone phosphorylation takes place during cellular response to DNA damage, when phosphorylated histone H2A(X) demarcates large chromatin domains around the site of DNA breakage. However, multiple studies have also shown that histone phosphorylation plays crucial roles in chromatin remodeling linked to other nuclear processes. In this review, we summarize the current knowledge of histone phosphorylation and describe the many kinases and phosphatases that regulate it. We discuss the key roles played by this histone mark in DNA repair, transcription and chromatin compaction during cell division and apoptosis. Additionally, we describe the intricate crosstalk that occurs between phosphorylation and other histone modifications and allows for sophisticated control over the chromatin remodeling processes.
    MeSH term(s) Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Chromatin/genetics ; Chromatin Assembly and Disassembly/genetics ; DNA Damage/genetics ; DNA Repair/genetics ; Histones/genetics ; Histones/metabolism ; Humans ; Phosphorylation ; Protein Processing, Post-Translational ; Transcription, Genetic
    Chemical Substances Chromatin ; H2AX protein, human ; Histones
    Language English
    Publishing date 2012-09-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 1559-2308
    ISSN (online) 1559-2308
    DOI 10.4161/epi.21975
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Epigenetic modifications in double-strand break DNA damage signaling and repair.

    Rossetto, Dorine / Truman, Andrew W / Kron, Stephen J / Côté, Jacques

    Clinical cancer research : an official journal of the American Association for Cancer Research

    2010  Volume 16, Issue 18, Page(s) 4543–4552

    Abstract: Factors involved in the cellular response to double-strand break (DSB) DNA damage have been identified as potential therapeutic targets that would greatly sensitize cancer cells to radiotherapy and genotoxic chemotherapy. These targets could disable the ... ...

    Abstract Factors involved in the cellular response to double-strand break (DSB) DNA damage have been identified as potential therapeutic targets that would greatly sensitize cancer cells to radiotherapy and genotoxic chemotherapy. These targets could disable the repair machinery and/or reinstate normal cell-cycle checkpoint leading to growth arrest, senescence, and apoptosis. It is now clear that a major aspect of the DNA damage response occurs through specific interactions with chromatin structure and its modulation. It implicates highly dynamic posttranslational modifications of histones that are critical for DNA damage recognition and/or signaling, repair of the lesion, and release of cell-cycle arrest. Therefore, drugs that target the enzymes responsible for these modifications, or the protein modules reading them, have very high therapeutic potential. This review presents the current state of knowledge on the different chromatin modifications and their roles in each step of eukaryotic DSB DNA damage response.
    MeSH term(s) Animals ; Chromatin Assembly and Disassembly/genetics ; Chromatin Assembly and Disassembly/physiology ; DNA Breaks, Double-Stranded ; DNA Damage/genetics ; DNA Repair/genetics ; Epigenesis, Genetic/physiology ; Humans ; Models, Biological ; Signal Transduction/genetics
    Language English
    Publishing date 2010-09-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1225457-5
    ISSN 1557-3265 ; 1078-0432
    ISSN (online) 1557-3265
    ISSN 1078-0432
    DOI 10.1158/1078-0432.CCR-10-0513
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome.

    Steunou, Anne-Lise / Cramet, Myriam / Rossetto, Dorine / Aristizabal, Maria J / Lacoste, Nicolas / Drouin, Simon / Côté, Valérie / Paquet, Eric / Utley, Rhea T / Krogan, Nevan / Robert, François / Kobor, Michael S / Côté, Jacques

    Molecular and cellular biology

    2016  Volume 36, Issue 22, Page(s) 2768–2781

    Abstract: Recognition of histone marks by reader modules is thought to be at the heart of epigenetic mechanisms. These protein domains are considered to function by targeting regulators to chromosomal loci carrying specific histone modifications. This is important ...

    Abstract Recognition of histone marks by reader modules is thought to be at the heart of epigenetic mechanisms. These protein domains are considered to function by targeting regulators to chromosomal loci carrying specific histone modifications. This is important for proper gene regulation as well as propagation of epigenetic information. The NuA4 acetyltransferase complex contains two of these reader modules, an H3K4me3-specific plant homeodomain (PHD) within the Yng2 subunit and an H3K36me2/3-specific chromodomain in the Eaf3 subunit. While each domain showed a close functional interaction with the respective histone mark that it recognizes, at the biochemical level, genetic level (as assessed with epistatic miniarray profile screens), and phenotypic level, cells with the combined loss of both readers showed greatly enhanced phenotypes. Chromatin immunoprecipitation coupled with next-generation sequencing experiments demonstrated that the Yng2 PHD specifically directs H4 acetylation near the transcription start site of highly expressed genes, while Eaf3 is important downstream on the body of the genes. Strikingly, the recruitment of the NuA4 complex to these loci was not significantly affected. Furthermore, RNA polymerase II occupancy was decreased only under conditions where both PHD and chromodomains were lost, generally in the second half of the gene coding regions. Altogether, these results argue that methylated histone reader modules in NuA4 are not responsible for its recruitment to the promoter or coding regions but, rather, are required to orient its acetyltransferase catalytic site to the methylated histone 3-bearing nucleosomes in the surrounding chromatin, cooperating to allow proper transition from transcription initiation to elongation.
    MeSH term(s) Acetylation ; Acetyltransferases/chemistry ; Acetyltransferases/genetics ; Acetyltransferases/metabolism ; Binding Sites ; Catalytic Domain ; Chromatin Immunoprecipitation ; Epigenesis, Genetic ; Genome, Fungal ; High-Throughput Nucleotide Sequencing ; Histone Acetyltransferases/chemistry ; Histone Acetyltransferases/metabolism ; Histone Code ; Histones/metabolism ; Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Analysis, DNA ; Transcription Initiation Site
    Chemical Substances Histones ; Saccharomyces cerevisiae Proteins ; Acetyltransferases (EC 2.3.1.-) ; Eaf3 protein, S cerevisiae (EC 2.3.1.-) ; Yng2 protein, S cerevisiae (EC 2.3.1.-) ; Histone Acetyltransferases (EC 2.3.1.48) ; NuA4 protein, S cerevisiae (EC 2.3.1.48) ; RNA Polymerase II (EC 2.7.7.-)
    Language English
    Publishing date 2016-10-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00112-16
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Eaf5/7/3 form a functionally independent NuA4 submodule linked to RNA polymerase II-coupled nucleosome recycling.

    Rossetto, Dorine / Cramet, Myriam / Wang, Alice Y / Steunou, Anne-Lise / Lacoste, Nicolas / Schulze, Julia M / Côté, Valérie / Monnet-Saksouk, Julie / Piquet, Sandra / Nourani, Amine / Kobor, Michael S / Côté, Jacques

    The EMBO journal

    2014  Volume 33, Issue 12, Page(s) 1397–1415

    Abstract: The NuA4 histone acetyltransferase complex is required for gene regulation, cell cycle progression, and DNA repair. Dissection of the 13-subunit complex reveals that the Eaf7 subunit bridges Eaf5 with Eaf3, a H3K36me3-binding chromodomain protein, and ... ...

    Abstract The NuA4 histone acetyltransferase complex is required for gene regulation, cell cycle progression, and DNA repair. Dissection of the 13-subunit complex reveals that the Eaf7 subunit bridges Eaf5 with Eaf3, a H3K36me3-binding chromodomain protein, and this Eaf5/7/3 trimer is anchored to NuA4 through Eaf5. This trimeric subcomplex represents a functional module, and a large portion exists in a native form outside the NuA4 complex. Gene-specific and genome-wide location analyses indicate that Eaf5/7/3 correlates with transcription activity and is enriched over the coding region. In agreement with a role in transcription elongation, the Eaf5/7/3 trimer interacts with phosphorylated RNA polymerase II and helps its progression. Loss of Eaf5/7/3 partially suppresses intragenic cryptic transcription arising in set2 mutants, supporting a role in nucleosome destabilization. On the other hand, loss of the trimer leads to an increase of replication-independent histone exchange over the coding region of transcribed genes. Taken together, these results lead to a model where Eaf5/7/3 associates with elongating polymerase to promote the disruption of nucleosomes in its path, but also their refolding in its wake.
    MeSH term(s) Acetyltransferases/metabolism ; Blotting, Western ; Chromatin Immunoprecipitation ; Gene Expression Regulation, Fungal/genetics ; Histone Acetyltransferases/metabolism ; Models, Biological ; Multiprotein Complexes/metabolism ; Nucleosomes/physiology ; RNA Polymerase II/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Multiprotein Complexes ; Nucleosomes ; Saccharomyces cerevisiae Proteins ; Acetyltransferases (EC 2.3.1.-) ; Eaf3 protein, S cerevisiae (EC 2.3.1.-) ; Eaf5 protein, S cerevisiae (EC 2.3.1.-) ; Eaf7 protein, S cerevisiae (EC 2.3.1.-) ; Histone Acetyltransferases (EC 2.3.1.48) ; NuA4 protein, S cerevisiae (EC 2.3.1.48) ; RNA Polymerase II (EC 2.7.7.-)
    Language English
    Publishing date 2014-05-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.201386433
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome

    Steunou, Anne-Lise / Cramet, Myriam / Rossetto, Dorine / Aristizabal, Maria J. / Lacoste, Nicolas / Drouin, Simon / Côté, Valérie / Paquet, Eric / Utley, Rhea T. / Krogan, Nevan / Robert, François / Kobor, Michael S. / Côté, Jacques

    Molecular and Cellular Biology. 2016 Nov. 1, v. 36, no. 22 p.2768-2781

    2016  

    Abstract: Recognition of histone marks by reader modules is thought to be at the heart of epigenetic mechanisms. These protein domains are considered to function by targeting regulators to chromosomal loci carrying specific histone modifications. This is important ...

    Abstract Recognition of histone marks by reader modules is thought to be at the heart of epigenetic mechanisms. These protein domains are considered to function by targeting regulators to chromosomal loci carrying specific histone modifications. This is important for proper gene regulation as well as propagation of epigenetic information. The NuA4 acetyltransferase complex contains two of these reader modules, an H3K4me3-specific plant homeodomain (PHD) within the Yng2 subunit and an H3K36me2/3-specific chromodomain in the Eaf3 subunit. While each domain showed a close functional interaction with the respective histone mark that it recognizes, at the biochemical level, genetic level (as assessed with epistatic miniarray profile screens), and phenotypic level, cells with the combined loss of both readers showed greatly enhanced phenotypes. Chromatin immunoprecipitation coupled with next-generation sequencing experiments demonstrated that the Yng2 PHD specifically directs H4 acetylation near the transcription start site of highly expressed genes, while Eaf3 is important downstream on the body of the genes. Strikingly, the recruitment of the NuA4 complex to these loci was not significantly affected. Furthermore, RNA polymerase II occupancy was decreased only under conditions where both PHD and chromodomains were lost, generally in the second half of the gene coding regions. Altogether, these results argue that methylated histone reader modules in NuA4 are not responsible for its recruitment to the promoter or coding regions but, rather, are required to orient its acetyltransferase catalytic site to the methylated histone 3-bearing nucleosomes in the surrounding chromatin, cooperating to allow proper transition from transcription initiation to elongation.
    Keywords DNA-directed RNA polymerase ; acetylation ; acetyltransferases ; active sites ; chromatin immunoprecipitation ; epigenetics ; epistasis ; histones ; methylation ; nucleosomes ; phenotype ; transcription initiation ; transcription initiation site
    Language English
    Dates of publication 2016-1101
    Size p. 2768-2781.
    Publishing place Taylor & Francis
    Document type Article ; Online
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00112-16
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: MYST protein acetyltransferase activity requires active site lysine autoacetylation.

    Yuan, Hua / Rossetto, Dorine / Mellert, Hestia / Dang, Weiwei / Srinivasan, Madhusudan / Johnson, Jamel / Hodawadekar, Santosh / Ding, Emily C / Speicher, Kaye / Abshiru, Nebiyu / Perry, Rocco / Wu, Jiang / Yang, Chao / Zheng, Y George / Speicher, David W / Thibault, Pierre / Verreault, Alain / Johnson, F Bradley / Berger, Shelley L /
    Sternglanz, Rolf / McMahon, Steven B / Côté, Jacques / Marmorstein, Ronen

    The EMBO journal

    2011  Volume 31, Issue 1, Page(s) 58–70

    Abstract: The MYST protein lysine acetyltransferases are evolutionarily conserved throughout eukaryotes and acetylate proteins to regulate diverse biological processes including gene regulation, DNA repair, cell-cycle regulation, stem cell homeostasis and ... ...

    Abstract The MYST protein lysine acetyltransferases are evolutionarily conserved throughout eukaryotes and acetylate proteins to regulate diverse biological processes including gene regulation, DNA repair, cell-cycle regulation, stem cell homeostasis and development. Here, we demonstrate that MYST protein acetyltransferase activity requires active site lysine autoacetylation. The X-ray crystal structures of yeast Esa1 (yEsa1/KAT5) bound to a bisubstrate H4K16CoA inhibitor and human MOF (hMOF/KAT8/MYST1) reveal that they are autoacetylated at a strictly conserved lysine residue in MYST proteins (yEsa1-K262 and hMOF-K274) in the enzyme active site. The structure of hMOF also shows partial occupancy of K274 in the unacetylated form, revealing that the side chain reorients to a position that engages the catalytic glutamate residue and would block cognate protein substrate binding. Consistent with the structural findings, we present mass spectrometry data and biochemical experiments to demonstrate that this lysine autoacetylation on yEsa1, hMOF and its yeast orthologue, ySas2 (KAT8) occurs in solution and is required for acetylation and protein substrate binding in vitro. We also show that this autoacetylation occurs in vivo and is required for the cellular functions of these MYST proteins. These findings provide an avenue for the autoposttranslational regulation of MYST proteins that is distinct from other acetyltransferases but draws similarities to the phosphoregulation of protein kinases.
    MeSH term(s) Acetylation ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Histone Acetyltransferases/genetics ; Histone Acetyltransferases/metabolism ; Histones/metabolism ; Humans ; Lysine/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Histones ; Saccharomyces cerevisiae Proteins ; Esa1 protein, S cerevisiae (EC 2.3.1.48) ; Histone Acetyltransferases (EC 2.3.1.48) ; KAT8 protein, human (EC 2.3.1.48) ; Sas2 protein, S cerevisiae (EC 2.3.1.48) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2011-10-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/emboj.2011.382
    Database MEDical Literature Analysis and Retrieval System OnLINE

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