Deimination stabilizes histone H2A/H2B dimers as revealed by electrospray ionization mass spectrometry

Journal of Mass Spectrometry : JMS
Shingo ShimoyamaSatoko Akashi

Abstract

Post-translational modifications of histones for reversibly changing chromosomal structures in promoter regions of genes are a prerequisite for transcriptional activation and repression of genes. Peptidylarginine deiminase 4 (PAD4), which mediates histone deimination by converting arginine residues into citrulline residues, is involved in the repression of gene transcription. However, the mechanism is still unclear. We studied the effects of deimination on the reconstituted histone H2A/H2B dimer structure by electrospray ionization mass spectrometry. Deimination of the H2A/H2B dimer by PAD4 indicated that the mass of H2A increased 2.7 Da, suggesting that two or three Arg residues of H2A were deiminated. Deimination of H2A monomer alone showed a 6.6-Da increase in mass. This indicates that about four more Arg residues of H2A are modified in the monomer state than in the H2A/H2B dimer state. Taking account of the finding that the unstructured portions in proteins are susceptible to deimination by PAD4, it is likely that H2A in the monomer state has a more flexible structure than that in the dimer state. Furthermore, analysis of the association of the H2A/H2B dimer in 2 or 4 M ammonium acetate with nano-electrospray ionization mas...Continue Reading

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Citations

Sep 1, 2011·Multiple Sclerosis : Clinical and Laboratory Research·Roberta CalabresePaola Caiafa
Jan 31, 2019·Journal of Mass Spectrometry : JMS·Bingbing XueZhixin Tian
Mar 11, 2015·Protein Science : a Publication of the Protein Society·Kazumi SaikusaSatoko Akashi
Jul 14, 2012·Journal of Mass Spectrometry : JMS·Mikko LaitaojaJanne Jänis
Nov 30, 2016·Frontiers in Immunology·Elisa CorsieroPaola Migliorini
Jun 5, 2018·Analytical Chemistry·Kazumi SaikusaSatoko Akashi

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