Class I histone deacetylases (HDAC1-3) are histone lysine delactylases

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

Standard

Class I histone deacetylases (HDAC1-3) are histone lysine delactylases. / Moreno-Yruela, Carlos; Zhang, Di; Wei, Wei; Bæk, Michael; Liu, Wenchao; Gao, Jinjun; Danková, Daniela; Nielsen, Alexander L.; Bolding, Julie E.; Yang, Lu; Jameson, Samuel T.; Wong, Jiemin; Olsen, Christian A.; Zhao, Yingming.

In: Science Advances, Vol. 8, No. 3, eabi6696, 2022.

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

Harvard

Moreno-Yruela, C, Zhang, D, Wei, W, Bæk, M, Liu, W, Gao, J, Danková, D, Nielsen, AL, Bolding, JE, Yang, L, Jameson, ST, Wong, J, Olsen, CA & Zhao, Y 2022, 'Class I histone deacetylases (HDAC1-3) are histone lysine delactylases', Science Advances, vol. 8, no. 3, eabi6696. https://doi.org/10.1126/sciadv.abi6696

APA

Moreno-Yruela, C., Zhang, D., Wei, W., Bæk, M., Liu, W., Gao, J., Danková, D., Nielsen, A. L., Bolding, J. E., Yang, L., Jameson, S. T., Wong, J., Olsen, C. A., & Zhao, Y. (2022). Class I histone deacetylases (HDAC1-3) are histone lysine delactylases. Science Advances, 8(3), [eabi6696]. https://doi.org/10.1126/sciadv.abi6696

Vancouver

Moreno-Yruela C, Zhang D, Wei W, Bæk M, Liu W, Gao J et al. Class I histone deacetylases (HDAC1-3) are histone lysine delactylases. Science Advances. 2022;8(3). eabi6696. https://doi.org/10.1126/sciadv.abi6696

Author

Moreno-Yruela, Carlos ; Zhang, Di ; Wei, Wei ; Bæk, Michael ; Liu, Wenchao ; Gao, Jinjun ; Danková, Daniela ; Nielsen, Alexander L. ; Bolding, Julie E. ; Yang, Lu ; Jameson, Samuel T. ; Wong, Jiemin ; Olsen, Christian A. ; Zhao, Yingming. / Class I histone deacetylases (HDAC1-3) are histone lysine delactylases. In: Science Advances. 2022 ; Vol. 8, No. 3.

Bibtex

@article{ea93bdb439f240378b76d9029117ca83,
title = "Class I histone deacetylases (HDAC1-3) are histone lysine delactylases",
abstract = "Lysine L-lactylation [K(L-la)] is a newly discovered histone mark stimulated under conditions of high glycolysis, such as the Warburg effect. K(L-la) is associated with functions that are different from the widely studied histone acetylation. While K(L-la) can be introduced by the acetyltransferase p300, histone delactylases enzymes remained unknown. Here, we report the systematic evaluation of zinc- and nicotinamide adenine dinucleotide-dependent histone deacetylases (HDACs) for their ability to cleave ε-N-L-lactyllysine marks. Our screens identified HDAC1-3 and SIRT1-3 as delactylases in vitro. HDAC1-3 show robust activity toward not only K(L-la) but also K(D-la) and diverse short-chain acyl modifications. We further confirmed the de-L-lactylase activity of HDACs 1 and 3 in cells. Together, these data suggest that histone lactylation is installed and removed by regulatory enzymes as opposed to spontaneous chemical reactivity. Our results therefore represent an important step toward full characterization of this pathway's regulatory elements.",
author = "Carlos Moreno-Yruela and Di Zhang and Wei Wei and Michael B{\ae}k and Wenchao Liu and Jinjun Gao and Daniela Dankov{\'a} and Nielsen, {Alexander L.} and Bolding, {Julie E.} and Lu Yang and Jameson, {Samuel T.} and Jiemin Wong and Olsen, {Christian A.} and Yingming Zhao",
note = "Funding Information: This work was supported by the Ministry of Science and Technology of China (2017YFA054201; to J.W.), the Danish Council for Independent Research-Natural Sciences (grant no. 6108-00166B; to C.A.O.), the Independent Research Fund Denmark-Technical and Production Sciences (grant no. 0136-00412B; to C.A.O.), the Carlsberg Foundation (2013-01-0333 and CF15-011; to C.A.O.), the European Research Council (ERC-CoG-725172-SIRFUNCT; to C.A.O.), the University of Chicago, Nancy and Leonard Florsheim family fund (to Y.Z.), and the NIH (grants GM135504, AR078555, DK118266, and CA251677; to Y.Z.). Publisher Copyright: Copyright {\textcopyright} 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).",
year = "2022",
doi = "10.1126/sciadv.abi6696",
language = "English",
volume = "8",
journal = "Science advances",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "3",

}

RIS

TY - JOUR

T1 - Class I histone deacetylases (HDAC1-3) are histone lysine delactylases

AU - Moreno-Yruela, Carlos

AU - Zhang, Di

AU - Wei, Wei

AU - Bæk, Michael

AU - Liu, Wenchao

AU - Gao, Jinjun

AU - Danková, Daniela

AU - Nielsen, Alexander L.

AU - Bolding, Julie E.

AU - Yang, Lu

AU - Jameson, Samuel T.

AU - Wong, Jiemin

AU - Olsen, Christian A.

AU - Zhao, Yingming

N1 - Funding Information: This work was supported by the Ministry of Science and Technology of China (2017YFA054201; to J.W.), the Danish Council for Independent Research-Natural Sciences (grant no. 6108-00166B; to C.A.O.), the Independent Research Fund Denmark-Technical and Production Sciences (grant no. 0136-00412B; to C.A.O.), the Carlsberg Foundation (2013-01-0333 and CF15-011; to C.A.O.), the European Research Council (ERC-CoG-725172-SIRFUNCT; to C.A.O.), the University of Chicago, Nancy and Leonard Florsheim family fund (to Y.Z.), and the NIH (grants GM135504, AR078555, DK118266, and CA251677; to Y.Z.). Publisher Copyright: Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

PY - 2022

Y1 - 2022

N2 - Lysine L-lactylation [K(L-la)] is a newly discovered histone mark stimulated under conditions of high glycolysis, such as the Warburg effect. K(L-la) is associated with functions that are different from the widely studied histone acetylation. While K(L-la) can be introduced by the acetyltransferase p300, histone delactylases enzymes remained unknown. Here, we report the systematic evaluation of zinc- and nicotinamide adenine dinucleotide-dependent histone deacetylases (HDACs) for their ability to cleave ε-N-L-lactyllysine marks. Our screens identified HDAC1-3 and SIRT1-3 as delactylases in vitro. HDAC1-3 show robust activity toward not only K(L-la) but also K(D-la) and diverse short-chain acyl modifications. We further confirmed the de-L-lactylase activity of HDACs 1 and 3 in cells. Together, these data suggest that histone lactylation is installed and removed by regulatory enzymes as opposed to spontaneous chemical reactivity. Our results therefore represent an important step toward full characterization of this pathway's regulatory elements.

AB - Lysine L-lactylation [K(L-la)] is a newly discovered histone mark stimulated under conditions of high glycolysis, such as the Warburg effect. K(L-la) is associated with functions that are different from the widely studied histone acetylation. While K(L-la) can be introduced by the acetyltransferase p300, histone delactylases enzymes remained unknown. Here, we report the systematic evaluation of zinc- and nicotinamide adenine dinucleotide-dependent histone deacetylases (HDACs) for their ability to cleave ε-N-L-lactyllysine marks. Our screens identified HDAC1-3 and SIRT1-3 as delactylases in vitro. HDAC1-3 show robust activity toward not only K(L-la) but also K(D-la) and diverse short-chain acyl modifications. We further confirmed the de-L-lactylase activity of HDACs 1 and 3 in cells. Together, these data suggest that histone lactylation is installed and removed by regulatory enzymes as opposed to spontaneous chemical reactivity. Our results therefore represent an important step toward full characterization of this pathway's regulatory elements.

U2 - 10.1126/sciadv.abi6696

DO - 10.1126/sciadv.abi6696

M3 - Journal article

C2 - 35044827

AN - SCOPUS:85123308988

VL - 8

JO - Science advances

JF - Science advances

SN - 2375-2548

IS - 3

M1 - eabi6696

ER -

ID: 291598911