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
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.
Protein Science
https://doi.org/10.1002/pro.2673
Dimers
Acetylation
Histone Code
Basic Amino Acids
Phase behavior
Deimination
Electrospray ionization
Histone H2A/H2B dimer
Ion mobilitymass spectrometry
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.
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.
@article{53314bf0814e4c75b36e851ddae351de,
title = "Charge-neutralization effect of the tail regions on the histone H2A/H2B dimer structure",
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.",
keywords = "Acetylation, Deimination, Electrospray ionization, Histone H2A/H2B dimer, Ion mobilitymass spectrometry",
author = "Kazumi Saikusa and Singo Shimoyama and Yuuki Asano and Aritaka Nagadoi and Mamoru Sato and Hitoshi Kurumizaka and Yoshifumi Nishimura and Satoko Akashi",
doi = "10.1002/pro.2673",
journal = "Protein Science",
publisher = "Cold Spring Harbor Laboratory Press",
T1 - Charge-neutralization effect of the tail regions on the histone H2A/H2B dimer structure
AU - Saikusa, Kazumi
AU - Shimoyama, Singo
AU - Asano, Yuuki
AU - Nagadoi, Aritaka
AU - Sato, Mamoru
AU - Kurumizaka, Hitoshi
AU - Nishimura, Yoshifumi
AU - Akashi, Satoko
N2 - 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.
AB - 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.
KW - Acetylation
KW - Deimination
KW - Electrospray ionization
KW - Histone H2A/H2B dimer
KW - Ion mobilitymass spectrometry
U2 - 10.1002/pro.2673
DO - 10.1002/pro.2673
JO - Protein Science
JF - Protein Science
10.1002/pro.2673