Synthetic Chromatin Acylation by an Artificial Catalyst System

Tadashi Ishiguro, Yoshifumi Amamoto, Kana Tanabe, Jiaan Liu, Hidetoshi Kajino, Akiko Fujimura, Yuki Aoi, Akihisa Osakabe, Naoki Horikoshi, Hitoshi Kurumizaka, Kenzo Yamatsugu, Shigehiro A. Kawashima, Motomu Kanai

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Histone acetylation is physiologically regulated by histone acetyltransferases (HATs) and histone deacetylases (HDACs) and constitutes a fundamental regulatory element in gene expression. New types of lysine acylation on histones have recently been identified, but it remains unclear how chromatin function is regulated by divergent types of histone acylation and various enzymes. Here, we report on an approach to modulating histone acylation states synthetically without relying on enzymes. We have developed an artificial catalyst system composed of nucleosome-binding catalysts and acyl donors, which preferentially acetylated or malonylated lysines on histone tails and suppressed intra- and inter-nucleosome interactions similarly to HATs. We demonstrate the utility of our approach by identifying a site-selectivity difference between two HDAC isoforms, Sirt1 and Sirt6, and comparing the functions of histone malonylation and acetylation. Our system is applicable to endogenous chromatin without genetic manipulation; thus, it can be used to dissect the complex regulation of chromatin.

Original languageEnglish
Pages (from-to)840-859
Number of pages20
JournalChem
Volume2
Issue number6
DOIs
Publication statusPublished - Jun 8 2017

Fingerprint

Acylation
Histones
Chromatin
Acetylation
catalyst
enzyme
Catalysts
Nucleosomes
Enzymes
gene expression
Histone Acetyltransferases
Histone Deacetylases
Gene expression
Lysine
Protein Isoforms
Gene Expression
regulation

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry
  • Environmental Chemistry
  • Chemical Engineering(all)
  • Biochemistry, medical
  • Materials Chemistry

Cite this

Ishiguro, T., Amamoto, Y., Tanabe, K., Liu, J., Kajino, H., Fujimura, A., ... Kanai, M. (2017). Synthetic Chromatin Acylation by an Artificial Catalyst System. Chem, 2(6), 840-859. https://doi.org/10.1016/j.chempr.2017.04.002

Synthetic Chromatin Acylation by an Artificial Catalyst System. / Ishiguro, Tadashi; Amamoto, Yoshifumi; Tanabe, Kana; Liu, Jiaan; Kajino, Hidetoshi; Fujimura, Akiko; Aoi, Yuki; Osakabe, Akihisa; Horikoshi, Naoki; Kurumizaka, Hitoshi; Yamatsugu, Kenzo; Kawashima, Shigehiro A.; Kanai, Motomu.

In: Chem, Vol. 2, No. 6, 08.06.2017, p. 840-859.

Research output: Contribution to journalArticle

Ishiguro, T, Amamoto, Y, Tanabe, K, Liu, J, Kajino, H, Fujimura, A, Aoi, Y, Osakabe, A, Horikoshi, N, Kurumizaka, H, Yamatsugu, K, Kawashima, SA & Kanai, M 2017, 'Synthetic Chromatin Acylation by an Artificial Catalyst System', Chem, vol. 2, no. 6, pp. 840-859. https://doi.org/10.1016/j.chempr.2017.04.002
Ishiguro T, Amamoto Y, Tanabe K, Liu J, Kajino H, Fujimura A et al. Synthetic Chromatin Acylation by an Artificial Catalyst System. Chem. 2017 Jun 8;2(6):840-859. https://doi.org/10.1016/j.chempr.2017.04.002
Ishiguro, Tadashi ; Amamoto, Yoshifumi ; Tanabe, Kana ; Liu, Jiaan ; Kajino, Hidetoshi ; Fujimura, Akiko ; Aoi, Yuki ; Osakabe, Akihisa ; Horikoshi, Naoki ; Kurumizaka, Hitoshi ; Yamatsugu, Kenzo ; Kawashima, Shigehiro A. ; Kanai, Motomu. / Synthetic Chromatin Acylation by an Artificial Catalyst System. In: Chem. 2017 ; Vol. 2, No. 6. pp. 840-859.
@article{e377cb03f1234d01ad231efcef453b74,
title = "Synthetic Chromatin Acylation by an Artificial Catalyst System",
abstract = "Histone acetylation is physiologically regulated by histone acetyltransferases (HATs) and histone deacetylases (HDACs) and constitutes a fundamental regulatory element in gene expression. New types of lysine acylation on histones have recently been identified, but it remains unclear how chromatin function is regulated by divergent types of histone acylation and various enzymes. Here, we report on an approach to modulating histone acylation states synthetically without relying on enzymes. We have developed an artificial catalyst system composed of nucleosome-binding catalysts and acyl donors, which preferentially acetylated or malonylated lysines on histone tails and suppressed intra- and inter-nucleosome interactions similarly to HATs. We demonstrate the utility of our approach by identifying a site-selectivity difference between two HDAC isoforms, Sirt1 and Sirt6, and comparing the functions of histone malonylation and acetylation. Our system is applicable to endogenous chromatin without genetic manipulation; thus, it can be used to dissect the complex regulation of chromatin.",
author = "Tadashi Ishiguro and Yoshifumi Amamoto and Kana Tanabe and Jiaan Liu and Hidetoshi Kajino and Akiko Fujimura and Yuki Aoi and Akihisa Osakabe and Naoki Horikoshi and Hitoshi Kurumizaka and Kenzo Yamatsugu and Kawashima, {Shigehiro A.} and Motomu Kanai",
year = "2017",
month = "6",
day = "8",
doi = "10.1016/j.chempr.2017.04.002",
language = "English",
volume = "2",
pages = "840--859",
journal = "Chem",
issn = "2451-9294",
publisher = "Elsevier Inc.",
number = "6",

}

TY - JOUR

T1 - Synthetic Chromatin Acylation by an Artificial Catalyst System

AU - Ishiguro, Tadashi

AU - Amamoto, Yoshifumi

AU - Tanabe, Kana

AU - Liu, Jiaan

AU - Kajino, Hidetoshi

AU - Fujimura, Akiko

AU - Aoi, Yuki

AU - Osakabe, Akihisa

AU - Horikoshi, Naoki

AU - Kurumizaka, Hitoshi

AU - Yamatsugu, Kenzo

AU - Kawashima, Shigehiro A.

AU - Kanai, Motomu

PY - 2017/6/8

Y1 - 2017/6/8

N2 - Histone acetylation is physiologically regulated by histone acetyltransferases (HATs) and histone deacetylases (HDACs) and constitutes a fundamental regulatory element in gene expression. New types of lysine acylation on histones have recently been identified, but it remains unclear how chromatin function is regulated by divergent types of histone acylation and various enzymes. Here, we report on an approach to modulating histone acylation states synthetically without relying on enzymes. We have developed an artificial catalyst system composed of nucleosome-binding catalysts and acyl donors, which preferentially acetylated or malonylated lysines on histone tails and suppressed intra- and inter-nucleosome interactions similarly to HATs. We demonstrate the utility of our approach by identifying a site-selectivity difference between two HDAC isoforms, Sirt1 and Sirt6, and comparing the functions of histone malonylation and acetylation. Our system is applicable to endogenous chromatin without genetic manipulation; thus, it can be used to dissect the complex regulation of chromatin.

AB - Histone acetylation is physiologically regulated by histone acetyltransferases (HATs) and histone deacetylases (HDACs) and constitutes a fundamental regulatory element in gene expression. New types of lysine acylation on histones have recently been identified, but it remains unclear how chromatin function is regulated by divergent types of histone acylation and various enzymes. Here, we report on an approach to modulating histone acylation states synthetically without relying on enzymes. We have developed an artificial catalyst system composed of nucleosome-binding catalysts and acyl donors, which preferentially acetylated or malonylated lysines on histone tails and suppressed intra- and inter-nucleosome interactions similarly to HATs. We demonstrate the utility of our approach by identifying a site-selectivity difference between two HDAC isoforms, Sirt1 and Sirt6, and comparing the functions of histone malonylation and acetylation. Our system is applicable to endogenous chromatin without genetic manipulation; thus, it can be used to dissect the complex regulation of chromatin.

UR - http://www.scopus.com/inward/record.url?scp=85020304533&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85020304533&partnerID=8YFLogxK

U2 - 10.1016/j.chempr.2017.04.002

DO - 10.1016/j.chempr.2017.04.002

M3 - Article

VL - 2

SP - 840

EP - 859

JO - Chem

JF - Chem

SN - 2451-9294

IS - 6

ER -