Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T

Hiroaki Tachiwana, Wataru Kagawa, Akihisa Osakabe, Koichiro Kawaguchi, Tatsuya Shiga, Yoko Hayashi-Takanaka, Hiroshi Kimura, Hitoshi Kurumizaka

    Research output: Contribution to journalArticle

    123 Citations (Scopus)

    Abstract

    A histone H3 variant, H3T, is highly expressed in the testis, suggesting that it may play an important role in the chromatin reorganization required for meiosis and/or spermatogenesis. In the present study, we found that the nucleosome containing human H3T is significantly unstable both in vitro and in vivo, as compared to the conventional nucleosome containing H3.1. The crystal structure of the H3T nucleosome revealed structural differences in the H3T regions on both ends of the central α2 helix, as compared to those of H3.1. The H3T-specific residues (Met71 and Val111) are the source of the structural differences observed between H3T and H3.1. A mutational analysis revealed that these residues are responsible for the reduced stability of the H3T-containing nucleosome. These physical and structural properties of the H3T-containing nucleosome may provide the basis of chromatin reorganization during spermatogenesis.

    Original languageEnglish
    Pages (from-to)10454-10459
    Number of pages6
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume107
    Issue number23
    DOIs
    Publication statusPublished - 2010 Jun 8

    Fingerprint

    Nucleosomes
    Histones
    Testis
    Spermatogenesis
    Chromatin
    Meiosis

    ASJC Scopus subject areas

    • General

    Cite this

    Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T. / Tachiwana, Hiroaki; Kagawa, Wataru; Osakabe, Akihisa; Kawaguchi, Koichiro; Shiga, Tatsuya; Hayashi-Takanaka, Yoko; Kimura, Hiroshi; Kurumizaka, Hitoshi.

    In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 107, No. 23, 08.06.2010, p. 10454-10459.

    Research output: Contribution to journalArticle

    Tachiwana, H, Kagawa, W, Osakabe, A, Kawaguchi, K, Shiga, T, Hayashi-Takanaka, Y, Kimura, H & Kurumizaka, H 2010, 'Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T', Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 23, pp. 10454-10459. https://doi.org/10.1073/pnas.1003064107
    Tachiwana, Hiroaki ; Kagawa, Wataru ; Osakabe, Akihisa ; Kawaguchi, Koichiro ; Shiga, Tatsuya ; Hayashi-Takanaka, Yoko ; Kimura, Hiroshi ; Kurumizaka, Hitoshi. / Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T. In: Proceedings of the National Academy of Sciences of the United States of America. 2010 ; Vol. 107, No. 23. pp. 10454-10459.
    @article{7677fcf8843840f5b00ce006f6278c57,
    title = "Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T",
    abstract = "A histone H3 variant, H3T, is highly expressed in the testis, suggesting that it may play an important role in the chromatin reorganization required for meiosis and/or spermatogenesis. In the present study, we found that the nucleosome containing human H3T is significantly unstable both in vitro and in vivo, as compared to the conventional nucleosome containing H3.1. The crystal structure of the H3T nucleosome revealed structural differences in the H3T regions on both ends of the central α2 helix, as compared to those of H3.1. The H3T-specific residues (Met71 and Val111) are the source of the structural differences observed between H3T and H3.1. A mutational analysis revealed that these residues are responsible for the reduced stability of the H3T-containing nucleosome. These physical and structural properties of the H3T-containing nucleosome may provide the basis of chromatin reorganization during spermatogenesis.",
    author = "Hiroaki Tachiwana and Wataru Kagawa and Akihisa Osakabe and Koichiro Kawaguchi and Tatsuya Shiga and Yoko Hayashi-Takanaka and Hiroshi Kimura and Hitoshi Kurumizaka",
    year = "2010",
    month = "6",
    day = "8",
    doi = "10.1073/pnas.1003064107",
    language = "English",
    volume = "107",
    pages = "10454--10459",
    journal = "Proceedings of the National Academy of Sciences of the United States of America",
    issn = "0027-8424",
    number = "23",

    }

    TY - JOUR

    T1 - Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T

    AU - Tachiwana, Hiroaki

    AU - Kagawa, Wataru

    AU - Osakabe, Akihisa

    AU - Kawaguchi, Koichiro

    AU - Shiga, Tatsuya

    AU - Hayashi-Takanaka, Yoko

    AU - Kimura, Hiroshi

    AU - Kurumizaka, Hitoshi

    PY - 2010/6/8

    Y1 - 2010/6/8

    N2 - A histone H3 variant, H3T, is highly expressed in the testis, suggesting that it may play an important role in the chromatin reorganization required for meiosis and/or spermatogenesis. In the present study, we found that the nucleosome containing human H3T is significantly unstable both in vitro and in vivo, as compared to the conventional nucleosome containing H3.1. The crystal structure of the H3T nucleosome revealed structural differences in the H3T regions on both ends of the central α2 helix, as compared to those of H3.1. The H3T-specific residues (Met71 and Val111) are the source of the structural differences observed between H3T and H3.1. A mutational analysis revealed that these residues are responsible for the reduced stability of the H3T-containing nucleosome. These physical and structural properties of the H3T-containing nucleosome may provide the basis of chromatin reorganization during spermatogenesis.

    AB - A histone H3 variant, H3T, is highly expressed in the testis, suggesting that it may play an important role in the chromatin reorganization required for meiosis and/or spermatogenesis. In the present study, we found that the nucleosome containing human H3T is significantly unstable both in vitro and in vivo, as compared to the conventional nucleosome containing H3.1. The crystal structure of the H3T nucleosome revealed structural differences in the H3T regions on both ends of the central α2 helix, as compared to those of H3.1. The H3T-specific residues (Met71 and Val111) are the source of the structural differences observed between H3T and H3.1. A mutational analysis revealed that these residues are responsible for the reduced stability of the H3T-containing nucleosome. These physical and structural properties of the H3T-containing nucleosome may provide the basis of chromatin reorganization during spermatogenesis.

    UR - http://www.scopus.com/inward/record.url?scp=77953805624&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=77953805624&partnerID=8YFLogxK

    U2 - 10.1073/pnas.1003064107

    DO - 10.1073/pnas.1003064107

    M3 - Article

    C2 - 20498094

    AN - SCOPUS:77953805624

    VL - 107

    SP - 10454

    EP - 10459

    JO - Proceedings of the National Academy of Sciences of the United States of America

    JF - Proceedings of the National Academy of Sciences of the United States of America

    SN - 0027-8424

    IS - 23

    ER -