Charge‐neutralization effect of the tail regions on the histone H2A/H2B dimer structure. (3rd April 2015)

• Record Type: Journal Article
• Authors: Saikusa, Kazumi; Shimoyama, Singo; Asano, Yuuki; Nagadoi, Aritaka; Sato, Mamoru; Kurumizaka, Hitoshi; Nishimura, Yoshifumi; Akashi, Satoko
• Is Part Of: Protein science. Volume 24:Number 8(2015:Aug.)
• Page Start: 1224
• Page End: 1231
• Publication Date: 2015-04-03
• Subjects: Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.2673
• Languages: English
• ISSNs: 0961-8368

Abstract

<abstract abstract-type="main"> <title>Abstract</title> <p>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.</p> </abstract>