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  1. Article ; Online: H2A.Z is involved in premature aging and DSB repair initiation in muscle fibers.

    Belotti, Edwige / Lacoste, Nicolas / Iftikhar, Arslan / Simonet, Thomas / Papin, Christophe / Osseni, Alexis / Streichenberger, Nathalie / Mari, Pierre-Olivier / Girard, Emmanuelle / Graies, Mohamed / Giglia-Mari, Giuseppina / Dimitrov, Stefan / Hamiche, Ali / Schaeffer, Laurent

    Nucleic acids research

    2024  Volume 52, Issue 6, Page(s) 3031–3049

    Abstract: Histone variants are key epigenetic players, but their functional and physiological roles remain poorly understood. Here, we show that depletion of the histone variant H2A.Z in mouse skeletal muscle causes oxidative stress, oxidation of proteins, ... ...

    Abstract Histone variants are key epigenetic players, but their functional and physiological roles remain poorly understood. Here, we show that depletion of the histone variant H2A.Z in mouse skeletal muscle causes oxidative stress, oxidation of proteins, accumulation of DNA damages, and both neuromuscular junction and mitochondria lesions that consequently lead to premature muscle aging and reduced life span. Investigation of the molecular mechanisms involved shows that H2A.Z is required to initiate DNA double strand break repair by recruiting Ku80 at DNA lesions. This is achieved via specific interactions of Ku80 vWA domain with H2A.Z. Taken as a whole, our data reveal that H2A.Z containing nucleosomes act as a molecular platform to bring together the proteins required to initiate and process DNA double strand break repair.
    MeSH term(s) Animals ; Mice ; Histones/genetics ; Histones/metabolism ; DNA Breaks, Double-Stranded ; Aging, Premature/genetics ; Nucleosomes ; DNA ; Muscle Fibers, Skeletal/metabolism
    Chemical Substances Histones ; Nucleosomes ; DNA (9007-49-2)
    Language English
    Publishing date 2024-01-28
    Publishing country England
    Document type Journal Article
    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/gkae020
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
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  2. Article ; Online: The CENP-A nucleosome: where and when it happens during the inner kinetochore's assembly

    Kale, Seyit / Boopathi, Ramachandran / Belloti, Edwige / Lone, Imtiaz Nizar / Graies, Mohamed / Schröder, Maria / Petrova, Maria / Papin, Christophe / Bednar, Jan / Ugrinova, Iva / Hamiche, Ali / Dimitrov, Stefan

    Trends in Biochemical Sciences.

    2023  

    Abstract: CENP-A is an essential histone variant that replaces the canonical H3 at the centromeres and marks these regions epigenetically. The CENP-A nucleosome is the specific building block of centromeric chromatin, and it is recognized by CENP-C and CENP-N, two ...

    Abstract CENP-A is an essential histone variant that replaces the canonical H3 at the centromeres and marks these regions epigenetically. The CENP-A nucleosome is the specific building block of centromeric chromatin, and it is recognized by CENP-C and CENP-N, two components of the constitutive centromere-associated network (CCAN), the first protein layer of the kinetochore. Recent proposals of the yeast and human (h)CCAN structures position the assembly on exposed DNA, suggesting an elusive spatiotemporal recognition. We summarize the data on the structural organization of the CENP-A nucleosome and the binding of CENP-C and CENP-N. The latter posits an apparent contradiction in engaging the CENP-A nucleosome versus the CCAN. We propose a reconciliatory model for the assembly of CCAN on centromeric chromatin.
    Keywords DNA ; histones ; humans ; kinetochores ; models ; nucleosomes ; yeasts ; mitosis ; chromatin ; histone variants ; CENP-A nucleosome ; CCAN complex
    Language English
    Publishing place Elsevier Ltd
    Document type Article ; Online
    Note Pre-press version
    ZDB-ID 194220-7
    ISSN 0968-0004 ; 0376-5067
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2023.07.010
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  3. Article: The CENP-A nucleosome: where and when it happens during the inner kinetochore's assembly.

    Kale, Seyit / Boopathi, Ramachandran / Belotti, Edwige / Lone, Imtiaz Nisar / Graies, Mohamed / Schröder, Maria / Petrova, Maria / Papin, Christophe / Bednar, Jan / Ugrinova, Iva / Hamiche, Ali / Dimitrov, Stefan

    Trends in biochemical sciences

    2023  Volume 48, Issue 10, Page(s) 849–859

    Abstract: CENP-A is an essential histone variant that replaces the canonical H3 at the centromeres and marks these regions epigenetically. The CENP-A nucleosome is the specific building block of centromeric chromatin, and it is recognized by CENP-C and CENP-N, two ...

    Abstract CENP-A is an essential histone variant that replaces the canonical H3 at the centromeres and marks these regions epigenetically. The CENP-A nucleosome is the specific building block of centromeric chromatin, and it is recognized by CENP-C and CENP-N, two components of the constitutive centromere-associated network (CCAN), the first protein layer of the kinetochore. Recent proposals of the yeast and human (h)CCAN structures position the assembly on exposed DNA, suggesting an elusive spatiotemporal recognition. We summarize the data on the structural organization of the CENP-A nucleosome and the binding of CENP-C and CENP-N. The latter posits an apparent contradiction in engaging the CENP-A nucleosome versus the CCAN. We propose a reconciliatory model for the assembly of CCAN on centromeric chromatin.
    MeSH term(s) Humans ; Centromere Protein A ; Chromatin ; Kinetochores ; Nucleosomes ; Saccharomyces cerevisiae
    Chemical Substances Centromere Protein A ; Chromatin ; Nucleosomes ; CENPA protein, human
    Language English
    Publishing date 2023-08-16
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2023.07.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1207: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

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