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Charge‐neutralization effect of the tail regions on the histone H 2 A / H 2 B dimer structure
Author(s) -
Saikusa Kazumi,
Shimoyama Singo,
Asano Yuuki,
Nagadoi Aritaka,
Sato Mamoru,
Kurumizaka Hitoshi,
Nishimura Yoshifumi,
Akashi Satoko
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2673
Subject(s) - dimer , chemistry , acetylation , histone , lysine , collision induced dissociation , histone octamer , dissociation (chemistry) , citrullination , neutralization , biophysics , arginine , biochemistry , amino acid , mass spectrometry , tandem mass spectrometry , nucleosome , chromatography , biology , organic chemistry , antibody , immunology , citrulline , gene
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.