Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II

Author:

Oishi Takumi12,Hatazawa Suguru1,Kujirai Tomoya13,Kato Junko1,Kobayashi Yuki1,Ogasawara Mitsuo1,Akatsu Munetaka12,Ehara Haruhiko3,Sekine Shun-ichi3,Hayashi Gosuke4,Takizawa Yoshimasa1,Kurumizaka Hitoshi123ORCID

Affiliation:

1. Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo , 1-1-1 Yayoi, Bunkyo-ku, Tokyo  113-0032 , Japan

2. Department of Biological Sciences, Graduate School of Science, The University of Tokyo , 1-1-1 Yayoi, Bunkyo-ku, Tokyo  113-0032 , Japan

3. Laboratory for Transcription Structural Biology, RIKEN Center for Biosystems Dynamics Research , 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama  230-0045 , Japan

4. Department of Biomolecular Engineering, Graduate School of Engineering, Nagoya University , Furo-cho, Chikusa-ku, Nagoya 464-8603 , Japan

Abstract

Abstract The N-terminal tails of histones protrude from the nucleosome core and are target sites for histone modifications, such as acetylation and methylation. Histone acetylation is considered to enhance transcription in chromatin. However, the contribution of the histone N-terminal tail to the nucleosome transcription by RNA polymerase II (RNAPII) has not been clarified. In the present study, we reconstituted nucleosomes lacking the N-terminal tail of each histone, H2A, H2B, H3 or H4, and performed RNAPII transcription assays. We found that the N-terminal tail of H3, but not H2A, H2B and H4, functions in RNAPII pausing at the SHL(-5) position of the nucleosome. Consistently, the RNAPII transcription assay also revealed that the nucleosome containing N-terminally acetylated H3 drastically alleviates RNAPII pausing at the SHL(-5) position. In addition, the H3 acetylated nucleosome produced increased amounts of the run-off transcript. These results provide important evidence that the H3 N-terminal tail plays a role in RNAPII pausing at the SHL(-5) position of the nucleosome, and its acetylation directly alleviates this nucleosome barrier.

Funder

JSPS

KAKENHI

JST

ERATO

AMED

Publisher

Oxford University Press (OUP)

Subject

Genetics

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