Regulation of RNA polymerase II activation by histone acetylation in single living cells

Timothy J. Stasevich (), Yoko Hayashi-Takanaka, Yuko Sato, Kazumitsu Maehara, Yasuyuki Ohkawa, Kumiko Sakata-Sogawa, Makio Tokunaga, Takahiro Nagase, Naohito Nozaki, James G. McNally and Hiroshi Kimura ()
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Timothy J. Stasevich: Graduate School of Frontier Biosciences, Osaka University, Osaka, 565-0871, Japan
Yoko Hayashi-Takanaka: Graduate School of Frontier Biosciences, Osaka University, Osaka, 565-0871, Japan
Yuko Sato: Graduate School of Frontier Biosciences, Osaka University, Osaka, 565-0871, Japan
Kazumitsu Maehara: Faculty of Medicine, Kyushu University, Fukuoka, 812-8582, Japan
Yasuyuki Ohkawa: Japan Science and Technology Agency (JST), Core Research for Evolutional Science and Technology (CREST), Kawaguchi, Saitama, 332-0012, Japan
Kumiko Sakata-Sogawa: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan
Makio Tokunaga: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan
Takahiro Nagase: Kazusa DNA Research Institute, Chiba, 292-0818, Japan
Naohito Nozaki: Mab Institute Inc., Sapporo, 001-0021, Japan
James G. McNally: Laboratory of Receptor Biology and Gene Expression, National Cancer Institute, National Institutes of Health
Hiroshi Kimura: Graduate School of Frontier Biosciences, Osaka University, Osaka, 565-0871, Japan

Nature, 2014, vol. 516, issue 7530, 272-275

Abstract: The interplay of histone acetylation and RNA polymerase II activity is investigated using fluorescence microscopy; acetylation of H3 at Lys 27 enhances the recruitment of a transcriptional activator and accelerates the transition of RNA polymerase II from initiation to elongation, thus indicating that histone acetylation has a causal effect on two distinct steps in transcription activation.

Date: 2014
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DOI: 10.1038/nature13714

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