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A novel histone exchange factor, protein phosphatase 2C, mediates the exchange and dephosphorylation of H2A–H2B

¹ Nuclear Function and Dynamics Unit and ² Biomolecular Characterization Unit, Horizontal Medical Research Organization, Graduate School of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan
³ Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724
⁴ Department of Molecular Genetics, National Institute of Genetics and the Graduate University for Advanced Studies, Mishima, Shizuoka 411-8540, Japan
⁵ Medical Research Council Molecular Haematology Unit, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, England, UK
⁶ Kanagawa Dental College, Yokosuka, Kanagawa 238-8580, Japan
⁷ Graduate School of Biological Science and Medical Research Institute, Tokyo Medical and Dental University, Bunkyo-ku, Tokyo 113-8510, Japan

Correspondence to Hiroshi Kimura: hkimura{at}hmro.med.kyoto-u.ac.jp

In eukaryotic nuclei, DNA is wrapped around a protein octamer composed of the core histones H2A, H2B, H3, and H4, forming nucleosomes as the fundamental units of chromatin. The modification and deposition of specific histone variants play key roles in chromatin function. In this study, we established an in vitro system based on permeabilized cells that allows the assembly and exchange of histones in situ. H2A and H2B, each tagged with green fluorescent protein (GFP), are incorporated into euchromatin by exchange independently of DNA replication, and H3.1-GFP is assembled into replicated chromatin, as found in living cells. By purifying the cellular factors that assist in the incorporation of H2A–H2B, we identified protein phosphatase (PP) 2C subtype (PP2C/PPM1G) as a histone chaperone that binds to and dephosphorylates H2A–H2B. The disruption of PP2C in chicken DT40 cells increased the sensitivity to caffeine, a reagent that disturbs DNA replication and damage checkpoints, suggesting the involvement of PP2C-mediated histone dephosphorylation and exchange in damage response or checkpoint recovery in higher eukaryotes.

Abbreviations used in this paper: AUT, acid-urea-Triton; FACT, facilitating chromatin transcription; Nap, nucleosome assembly protein; PB, physiological buffer; PP, protein phosphatase.

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