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  1. Article ; Online: Hydrolysis of ADP-Ribosylation by Macrodomains.

    Posavec Marjanovic, Melanija / Jankevicius, Gytis / Ahel, Ivan

    Methods in molecular biology (Clifton, N.J.)

    2018  Volume 1813, Page(s) 215–223

    Abstract: ADP-ribosylation is the process of transferring the ADP-ribose moiety from ... ...

    Abstract ADP-ribosylation is the process of transferring the ADP-ribose moiety from NAD
    MeSH term(s) ADP Ribose Transferases/chemistry ; ADP Ribose Transferases/genetics ; ADP-Ribosylation ; Adenosine Diphosphate Ribose/chemistry ; Hydrolysis ; Models, Molecular ; Molecular Biology/methods ; NAD/chemistry ; NAD/genetics ; Protein Domains ; Protein Processing, Post-Translational ; Proteins/chemistry ; Proteins/genetics
    Chemical Substances Proteins ; NAD (0U46U6E8UK) ; Adenosine Diphosphate Ribose (20762-30-5) ; ADP Ribose Transferases (EC 2.4.2.-)
    Language English
    Publishing date 2018-08-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-8588-3_14
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: PARP, transcription and chromatin modeling.

    Posavec Marjanović, Melanija / Crawford, Kerryanne / Ahel, Ivan

    Seminars in cell & developmental biology

    2016  Volume 63, Page(s) 102–113

    Abstract: Compaction mode of chromatin and chromatin highly organised structures regulate gene expression. Posttranslational modifications, histone variants and chromatin remodelers modulate the compaction, structure and therefore function of specific regions of ... ...

    Abstract Compaction mode of chromatin and chromatin highly organised structures regulate gene expression. Posttranslational modifications, histone variants and chromatin remodelers modulate the compaction, structure and therefore function of specific regions of chromatin. The generation of poly(ADP-ribose) (PAR) is emerging as one of the key signalling events on sites undergoing chromatin structure modulation. PAR is generated locally in response to stresses. These include genotoxic stress but also differentiation signals, metabolic and hormonal cues. A pictures emerges in which transient PAR formation is essential to orchestrate chromatin remodelling and transcription factors allowing the cell to adapt to alteration in its environment. This review summarizes the diverse factors of ADP-ribosylation in the adaptive regulation of chromatin structure and transcription.
    MeSH term(s) ADP-Ribosylation ; Animals ; Chromatin/metabolism ; Chromatin Assembly and Disassembly ; DNA Repair/genetics ; Humans ; Poly(ADP-ribose) Polymerases/metabolism ; Transcription, Genetic
    Chemical Substances Chromatin ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
    Language English
    Publishing date 2016-09-24
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2016.09.014
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  3. Article ; Online: The high mobility group protein HMG20A cooperates with the histone reader PHF14 to modulate TGFβ and Hippo pathways.

    Gómez-Marín, Elena / Posavec-Marjanović, Melanija / Zarzuela, Laura / Basurto-Cayuela, Laura / Guerrero-Martínez, José A / Arribas, Gonzalo / Yerbes, Rosario / Ceballos-Chávez, María / Rodríguez-Paredes, Manuel / Tomé, Mercedes / Durán, Raúl V / Buschbeck, Marcus / Reyes, José C

    Nucleic acids research

    2022  Volume 50, Issue 17, Page(s) 9838–9857

    Abstract: High mobility group (HMG) proteins are chromatin regulators with essential functions in development, cell differentiation and cell proliferation. The protein HMG20A is predicted by the AlphaFold2 software to contain three distinct structural elements, ... ...

    Abstract High mobility group (HMG) proteins are chromatin regulators with essential functions in development, cell differentiation and cell proliferation. The protein HMG20A is predicted by the AlphaFold2 software to contain three distinct structural elements, which we have functionally characterized: i) an amino-terminal, intrinsically disordered domain with transactivation activity; ii) an HMG box with higher binding affinity for double-stranded, four-way-junction DNA than for linear DNA; and iii) a long coiled-coil domain. Our proteomic study followed by a deletion analysis and structural modeling demonstrates that HMG20A forms a complex with the histone reader PHF14, via the establishment of a two-stranded alpha-helical coiled-coil structure. siRNA-mediated knockdown of either PHF14 or HMG20A in MDA-MB-231 cells causes similar defects in cell migration, invasion and homotypic cell-cell adhesion ability, but neither affects proliferation. Transcriptomic analyses demonstrate that PHF14 and HMG20A share a large subset of targets. We show that the PHF14-HMG20A complex modulates the Hippo pathway through a direct interaction with the TEAD1 transcription factor. PHF14 or HMG20A deficiency increases epithelial markers, including E-cadherin and the epithelial master regulator TP63 and impaired normal TGFβ-trigged epithelial-to-mesenchymal transition. Taken together, these data indicate that PHF14 and HMG20A cooperate in regulating several pathways involved in epithelial-mesenchymal plasticity.
    MeSH term(s) Cadherins/genetics ; Cadherins/metabolism ; Cell Line, Tumor ; Chromatin ; High Mobility Group Proteins/metabolism ; Hippo Signaling Pathway ; Histones/metabolism ; Humans ; Nuclear Proteins/metabolism ; Proteomics ; RNA, Small Interfering ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transforming Growth Factor beta/genetics
    Chemical Substances Cadherins ; Chromatin ; HMG20A protein, human ; High Mobility Group Proteins ; Histones ; Nuclear Proteins ; PHF14 protein, human ; RNA, Small Interfering ; Transcription Factors ; Transforming Growth Factor beta
    Language English
    Publishing date 2022-09-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkac766
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  4. Article ; Online: The Histone Variant MacroH2A1 Regulates Key Genes for Myogenic Cell Fusion in a Splice-Isoform Dependent Manner.

    Hurtado-Bagès, Sarah / Posavec Marjanovic, Melanija / Valero, Vanesa / Malinverni, Roberto / Corujo, David / Bouvet, Philippe / Lavigne, Anne-Claire / Bystricky, Kerstin / Buschbeck, Marcus

    Cells

    2020  Volume 9, Issue 5

    Abstract: MacroH2A histone variants have functions in differentiation, somatic cell reprogramming and cancer. However, at present, it is not clear how macroH2As affect gene regulation to exert these functions. We have parted from the initial observation that loss ... ...

    Abstract MacroH2A histone variants have functions in differentiation, somatic cell reprogramming and cancer. However, at present, it is not clear how macroH2As affect gene regulation to exert these functions. We have parted from the initial observation that loss of total macroH2A1 led to a change in the morphology of murine myotubes differentiated ex vivo. The fusion of myoblasts to myotubes is a key process in embryonic myogenesis and highly relevant for muscle regeneration after acute or chronic injury. We have focused on this physiological process, to investigate the functions of the two splice isoforms of macroH2A1. Individual perturbation of the two isoforms in myotubes forming in vitro from myogenic C2C12 cells showed an opposing phenotype, with macroH2A1.1 enhancing, and macroH2A1.2 reducing, fusion. Differential regulation of a subset of fusion-related genes encoding components of the extracellular matrix and cell surface receptors for adhesion correlated with these phenotypes. We describe, for the first time, splice isoform-specific phenotypes for the histone variant macroH2A1 in a physiologic process and provide evidence for a novel underlying molecular mechanism of gene regulation.
    MeSH term(s) Animals ; Cell Adhesion/genetics ; Cell Differentiation/genetics ; Cell Fusion/methods ; Cell Line ; Chromatin/genetics ; Extracellular Matrix/metabolism ; Histones/genetics ; Histones/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Muscle Development/genetics ; Muscle Development/physiology ; Myoblasts/metabolism ; Protein Isoforms/metabolism
    Chemical Substances Chromatin ; Histones ; Macroh2a1 protein, mouse ; Protein Isoforms ; macroH2A histone
    Language English
    Publishing date 2020-04-30
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells9051109
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  5. Article ; Online: MacroH2A histone variants maintain nuclear organization and heterochromatin architecture.

    Douet, Julien / Corujo, David / Malinverni, Roberto / Renauld, Justine / Sansoni, Viola / Posavec Marjanović, Melanija / Cantariño, Neus / Valero, Vanesa / Mongelard, Fabien / Bouvet, Philippe / Imhof, Axel / Thiry, Marc / Buschbeck, Marcus

    Journal of cell science

    2017  Volume 130, Issue 9, Page(s) 1570–1582

    Abstract: Genetic loss-of-function studies on development, cancer and somatic cell reprogramming have suggested that the group of macroH2A histone variants might function through stabilizing the differentiated state by a yet unknown mechanism. Here, we present ... ...

    Abstract Genetic loss-of-function studies on development, cancer and somatic cell reprogramming have suggested that the group of macroH2A histone variants might function through stabilizing the differentiated state by a yet unknown mechanism. Here, we present results demonstrating that macroH2A variants have a major function in maintaining nuclear organization and heterochromatin architecture. Specifically, we find that a substantial amount of macroH2A is associated with heterochromatic repeat sequences. We further identify macroH2A on sites of interstitial heterochromatin decorated by histone H3 trimethylated on K9 (H3K9me3). Loss of macroH2A leads to major defects in nuclear organization, including reduced nuclear circularity, disruption of nucleoli and a global loss of dense heterochromatin. Domains formed by DNA repeat sequences are disorganized, expanded and fragmented, and mildly re-expressed when depleted of macroH2A. At the molecular level, we find that macroH2A is required for the interaction of repeat sequences with the nucleostructural protein lamin B1. Taken together, our results argue that a major function of macroH2A histone variants is to link nucleosome composition to higher-order chromatin architecture.
    MeSH term(s) Cell Nucleolus/metabolism ; Cell Nucleolus/ultrastructure ; HEK293 Cells ; Hep G2 Cells ; Heterochromatin/metabolism ; Heterochromatin/ultrastructure ; Histones/metabolism ; Humans ; Lamin Type B/metabolism ; Lysine/metabolism ; Male ; Methylation ; Protein Binding
    Chemical Substances Heterochromatin ; Histones ; Lamin Type B ; macroH2A histone ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2017-03-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.199216
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  6. Article ; Online: Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor.

    Lalić, Jasna / Posavec Marjanović, Melanija / Palazzo, Luca / Perina, Dragutin / Sabljić, Igor / Žaja, Roko / Colby, Thomas / Pleše, Bruna / Halasz, Mirna / Jankevicius, Gytis / Bucca, Giselda / Ahel, Marijan / Matić, Ivan / Ćetković, Helena / Luić, Marija / Mikoč, Andreja / Ahel, Ivan

    The Journal of biological chemistry

    2016  Volume 291, Issue 44, Page(s) 23175–23187

    Abstract: ADP-ribosylation is a post-translational modification that can alter the physical and chemical properties of target proteins and that controls many important cellular processes. Macrodomains are evolutionarily conserved structural domains that bind ADP- ... ...

    Abstract ADP-ribosylation is a post-translational modification that can alter the physical and chemical properties of target proteins and that controls many important cellular processes. Macrodomains are evolutionarily conserved structural domains that bind ADP-ribose derivatives and are found in proteins with diverse cellular functions. Some proteins from the macrodomain family can hydrolyze ADP-ribosylated substrates and therefore reverse this post-translational modification. Bacteria and Streptomyces, in particular, are known to utilize protein ADP-ribosylation, yet very little is known about their enzymes that synthesize and remove this modification. We have determined the crystal structure and characterized, both biochemically and functionally, the macrodomain protein SCO6735 from Streptomyces coelicolor This protein is a member of an uncharacterized subfamily of macrodomain proteins. Its crystal structure revealed a highly conserved macrodomain fold. We showed that SCO6735 possesses the ability to hydrolyze PARP-dependent protein ADP-ribosylation. Furthermore, we showed that expression of this protein is induced upon DNA damage and that deletion of this protein in S. coelicolor increases antibiotic production. Our results provide the first insights into the molecular basis of its action and impact on Streptomyces metabolism.
    MeSH term(s) Adenosine Diphosphate Ribose/metabolism ; Anti-Bacterial Agents/biosynthesis ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; DNA Damage ; Protein Processing, Post-Translational ; Streptomyces coelicolor/chemistry ; Streptomyces coelicolor/genetics ; Streptomyces coelicolor/metabolism
    Chemical Substances Anti-Bacterial Agents ; Bacterial Proteins ; Adenosine Diphosphate Ribose (20762-30-5)
    Language English
    Publishing date 2016-09-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M116.721894
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  7. Article ; Online: MacroH2A1.1 regulates mitochondrial respiration by limiting nuclear NAD

    Posavec Marjanović, Melanija / Hurtado-Bagès, Sarah / Lassi, Maximilian / Valero, Vanesa / Malinverni, Roberto / Delage, Hélène / Navarro, Miriam / Corujo, David / Guberovic, Iva / Douet, Julien / Gama-Perez, Pau / Garcia-Roves, Pablo M / Ahel, Ivan / Ladurner, Andreas G / Yanes, Oscar / Bouvet, Philippe / Suelves, Mònica / Teperino, Raffaele / Pospisilik, J Andrew /
    Buschbeck, Marcus

    Nature structural & molecular biology

    2017  Volume 24, Issue 11, Page(s) 902–910

    Abstract: Histone variants are structural components of eukaryotic chromatin that can replace replication-coupled histones in the nucleosome. The histone variant macroH2A1.1 contains a macrodomain capable of binding ... ...

    Abstract Histone variants are structural components of eukaryotic chromatin that can replace replication-coupled histones in the nucleosome. The histone variant macroH2A1.1 contains a macrodomain capable of binding NAD
    MeSH term(s) Animals ; Cell Nucleus/metabolism ; Cell Respiration ; Gene Expression Regulation, Developmental ; Histones/metabolism ; Mice/embryology ; Mitochondria/metabolism ; Muscle Development ; NAD/metabolism
    Chemical Substances Histones ; macroH2A histone ; NAD (0U46U6E8UK)
    Language English
    Publishing date 2017-10-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/nsmb.3481
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    Zs.MG 56: Show issues

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