Charge-neutralization effect of the tail regions on the histone H2A/H2B dimer structure

Kazumi Saikusa, Singo Shimoyama, Yuuki Asano, Aritaka Nagadoi, Mamoru Sato, Hitoshi Kurumizaka, Yoshifumi Nishimura, Satoko Akashi

    Research output: Contribution to journalArticle

    3 Citations (Scopus)

    Abstract

    It is well known that various modifications of histone tails play important roles in the regulation of transcription initiation. In this study, some lysine (Lys) and arginine (Arg) residues were acetylated and deiminated, respectively, in the histone H2A/H2B dimer, and charge-neutralization effects on the dimer structure were studied by native mass spectrometry. Given that both acetylation and deimination neutralize the positive charges of basic amino acid residues, it had been expected that these modifications would correspondingly affect the gas-phase behavior of the histone H2A/H2B dimer. Contrary to this expectation, it was found that Arg deimination led to greater difficulty of dissociation of the dimer by gas-phase collision, whereas acetylation of Lys residues did not cause such a drastic change in the dimer stability. In contrast, ion mobility-mass spectrometry (IM-MS) experiments showed that arrival times in the mobility cell both of acetylated and of deiminated dimer ions changed little from those of the unmodified dimer ions, indicating that the sizes of the dimer ions did not change by modification. Charge neutralization of Arg, basicity of which is higher than Lys, might have triggered some alteration of the dimer structure that cannot be found in IM-MS but can be detected by collision in the gas phase.

    Original languageEnglish
    Pages (from-to)1224-1231
    Number of pages8
    JournalProtein Science
    Volume24
    Issue number8
    DOIs
    Publication statusPublished - 2015

    Fingerprint

    Dimers
    Histones
    Ions
    Lysine
    Arginine
    Mass Spectrometry
    Gases
    Acetylation
    Histone Code
    Mass spectrometry
    Basic Amino Acids
    Transcription
    Phase behavior
    Alkalinity

    Keywords

    • Acetylation
    • Deimination
    • Electrospray ionization
    • Histone H2A/H2B dimer
    • Ion mobilitymass spectrometry

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology

    Cite this

    Saikusa, K., Shimoyama, S., Asano, Y., Nagadoi, A., Sato, M., Kurumizaka, H., ... Akashi, S. (2015). Charge-neutralization effect of the tail regions on the histone H2A/H2B dimer structure. Protein Science, 24(8), 1224-1231. https://doi.org/10.1002/pro.2673

    Charge-neutralization effect of the tail regions on the histone H2A/H2B dimer structure. / Saikusa, Kazumi; Shimoyama, Singo; Asano, Yuuki; Nagadoi, Aritaka; Sato, Mamoru; Kurumizaka, Hitoshi; Nishimura, Yoshifumi; Akashi, Satoko.

    In: Protein Science, Vol. 24, No. 8, 2015, p. 1224-1231.

    Research output: Contribution to journalArticle

    Saikusa, K, Shimoyama, S, Asano, Y, Nagadoi, A, Sato, M, Kurumizaka, H, Nishimura, Y & Akashi, S 2015, 'Charge-neutralization effect of the tail regions on the histone H2A/H2B dimer structure', Protein Science, vol. 24, no. 8, pp. 1224-1231. https://doi.org/10.1002/pro.2673
    Saikusa K, Shimoyama S, Asano Y, Nagadoi A, Sato M, Kurumizaka H et al. Charge-neutralization effect of the tail regions on the histone H2A/H2B dimer structure. Protein Science. 2015;24(8):1224-1231. https://doi.org/10.1002/pro.2673
    Saikusa, Kazumi ; Shimoyama, Singo ; Asano, Yuuki ; Nagadoi, Aritaka ; Sato, Mamoru ; Kurumizaka, Hitoshi ; Nishimura, Yoshifumi ; Akashi, Satoko. / Charge-neutralization effect of the tail regions on the histone H2A/H2B dimer structure. In: Protein Science. 2015 ; Vol. 24, No. 8. pp. 1224-1231.
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