前原さんの論文がSci Rep.に発表されました。（大阪大学との共同研究）
Sci Rep. 2016 Apr 11;6:24318. doi: 10.1038/srep24318.
Histone H4 lysine 20 acetylation is associated with gene repression in human cells.
Kaimori JY1,2*, Maehara K3*, Hayashi-Takanaka Y4,5,6, Harada A3, Fukuda M7, Yamamoto S2, Ichimaru N1, Umehara T8, Yokoyama S9, Matsuda R10, Ikura T10, Nagao K11, Obuse C11, Nozaki N12, Takahara S1, Takao T7, Ohkawa Y3,6, Kimura H4,5,6, Isaka Y2.
*These authors contributed equally to this work.
1Department of Advanced Technology of Transplantation, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
2Department of Nephrology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
3Division of Transcriptomics, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.
4Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.
5Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan.
6CREST, JST, 4-1-8, Honcho, Kawaguchi, Saitama 332-0012, Japan.
7Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan.
8RIKEN Center for Life Science Technologies, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
9RIKEN Structural Biology Laboratory, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
10Radiation Biology Center, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
11Graduate School of Life Science, Hokkaido University, Kita 21 Nishi 12, Sapporo 001-0021, Japan.
12MAB Institute Inc., Kita 21 Nishi 12, Sapporo 001-0021, Japan.
Abstract
Histone acetylation is generally associated with gene activation and chromatin decondensation. Recent mass spectrometry analysis has revealed that histone H4 lysine 20, a major methylation site, can also be acetylated. To understand the function of H4 lysine 20 acetylation (H4K20ac), we have developed a specific monoclonal antibody and performed ChIP-seq analysis using HeLa-S3 cells. H4K20ac was enriched around the transcription start sites (TSSs) of minimally expressed genes and in the gene body of expressed genes, in contrast to most histone acetylation being enriched around the TSSs of expressed genes. The distribution of H4K20ac showed little correlation with known histone modifications, including histone H3 methylations. A motif search in H4K20ac-enriched sequences, together with transcription factor binding profiles based on ENCODE ChIP-seq data, revealed that most transcription activators are excluded from H4K20ac-enriched genes and a transcription repressor NRSF/REST co-localized with H4K20ac. These results suggest that H4K20ac is a unique acetylation mark associated with gene repression.