Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription. / Kollenstart, Leonie; de Groot, Anton J L; Janssen, George M C; Cheng, Xue; Vreeken, Kees; Martino, Fabrizio; Côté, Jacques; van Veelen, Peter A; van Attikum, Haico.

In: The Journal of Biological Chemistry, Vol. 294, No. 52, 27.12.2019, p. 20122-20134.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kollenstart, L, de Groot, AJL, Janssen, GMC, Cheng, X, Vreeken, K, Martino, F, Côté, J, van Veelen, PA & van Attikum, H 2019, 'Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription', The Journal of Biological Chemistry, vol. 294, no. 52, pp. 20122-20134. https://doi.org/10.1074/jbc.RA119.010302

APA

Kollenstart, L., de Groot, A. J. L., Janssen, G. M. C., Cheng, X., Vreeken, K., Martino, F., Côté, J., van Veelen, P. A., & van Attikum, H. (2019). Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription. The Journal of Biological Chemistry, 294(52), 20122-20134. https://doi.org/10.1074/jbc.RA119.010302

Vancouver

Kollenstart L, de Groot AJL, Janssen GMC, Cheng X, Vreeken K, Martino F et al. Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription. The Journal of Biological Chemistry. 2019 Dec 27;294(52):20122-20134. https://doi.org/10.1074/jbc.RA119.010302

Author

Kollenstart, Leonie ; de Groot, Anton J L ; Janssen, George M C ; Cheng, Xue ; Vreeken, Kees ; Martino, Fabrizio ; Côté, Jacques ; van Veelen, Peter A ; van Attikum, Haico. / Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription. In: The Journal of Biological Chemistry. 2019 ; Vol. 294, No. 52. pp. 20122-20134.

Bibtex

@article{c6ee5b413c1946d4b3ca7ea8515dac2a,
title = "Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription",
abstract = "Histone post-translational modifications (PTMs) are critical for processes such as transcription. The more notable among these are the nonacetyl histone lysine acylation modifications such as crotonylation, butyrylation, and succinylation. However, the biological relevance of these PTMs is not fully understood because their regulation is largely unknown. Here, we set out to investigate whether the main histone acetyltransferases in budding yeast, Gcn5 and Esa1, possess crotonyltransferase activity. In vitro studies revealed that the Gcn5-Ada2-Ada3 (ADA) and Esa1-Yng2-Epl1 (Piccolo NuA4) histone acetyltransferase complexes have the capacity to crotonylate histones. Mass spectrometry analysis revealed that ADA and Piccolo NuA4 crotonylate lysines in the N-terminal tails of histone H3 and H4, respectively. Functionally, we show that crotonylation selectively affects gene transcription in vivo in a manner dependent on Gcn5 and Esa1. Thus, we identify the Gcn5- and Esa1-containing ADA and Piccolo NuA4 complexes as bona fide crotonyltransferases that promote crotonylation-dependent transcription.",
author = "Leonie Kollenstart and {de Groot}, {Anton J L} and Janssen, {George M C} and Xue Cheng and Kees Vreeken and Fabrizio Martino and Jacques C{\^o}t{\'e} and {van Veelen}, {Peter A} and {van Attikum}, Haico",
note = "{\textcopyright} 2019 Kollenstart et al.",
year = "2019",
month = dec,
day = "27",
doi = "10.1074/jbc.RA119.010302",
language = "English",
volume = "294",
pages = "20122--20134",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "52",

}

RIS

TY - JOUR

T1 - Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription

AU - Kollenstart, Leonie

AU - de Groot, Anton J L

AU - Janssen, George M C

AU - Cheng, Xue

AU - Vreeken, Kees

AU - Martino, Fabrizio

AU - Côté, Jacques

AU - van Veelen, Peter A

AU - van Attikum, Haico

N1 - © 2019 Kollenstart et al.

PY - 2019/12/27

Y1 - 2019/12/27

N2 - Histone post-translational modifications (PTMs) are critical for processes such as transcription. The more notable among these are the nonacetyl histone lysine acylation modifications such as crotonylation, butyrylation, and succinylation. However, the biological relevance of these PTMs is not fully understood because their regulation is largely unknown. Here, we set out to investigate whether the main histone acetyltransferases in budding yeast, Gcn5 and Esa1, possess crotonyltransferase activity. In vitro studies revealed that the Gcn5-Ada2-Ada3 (ADA) and Esa1-Yng2-Epl1 (Piccolo NuA4) histone acetyltransferase complexes have the capacity to crotonylate histones. Mass spectrometry analysis revealed that ADA and Piccolo NuA4 crotonylate lysines in the N-terminal tails of histone H3 and H4, respectively. Functionally, we show that crotonylation selectively affects gene transcription in vivo in a manner dependent on Gcn5 and Esa1. Thus, we identify the Gcn5- and Esa1-containing ADA and Piccolo NuA4 complexes as bona fide crotonyltransferases that promote crotonylation-dependent transcription.

AB - Histone post-translational modifications (PTMs) are critical for processes such as transcription. The more notable among these are the nonacetyl histone lysine acylation modifications such as crotonylation, butyrylation, and succinylation. However, the biological relevance of these PTMs is not fully understood because their regulation is largely unknown. Here, we set out to investigate whether the main histone acetyltransferases in budding yeast, Gcn5 and Esa1, possess crotonyltransferase activity. In vitro studies revealed that the Gcn5-Ada2-Ada3 (ADA) and Esa1-Yng2-Epl1 (Piccolo NuA4) histone acetyltransferase complexes have the capacity to crotonylate histones. Mass spectrometry analysis revealed that ADA and Piccolo NuA4 crotonylate lysines in the N-terminal tails of histone H3 and H4, respectively. Functionally, we show that crotonylation selectively affects gene transcription in vivo in a manner dependent on Gcn5 and Esa1. Thus, we identify the Gcn5- and Esa1-containing ADA and Piccolo NuA4 complexes as bona fide crotonyltransferases that promote crotonylation-dependent transcription.

U2 - 10.1074/jbc.RA119.010302

DO - 10.1074/jbc.RA119.010302

M3 - Journal article

C2 - 31699900

VL - 294

SP - 20122

EP - 20134

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 52

ER -

ID: 242624112