Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation

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

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Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation. / Hansen, Bogi Karbech; Gupta, Rajat; Baldus, Linda; Lyon, David; Narita, Takeo; Lammers, Michael; Choudhary, Chunaram; Weinert, Brian T.

In: Nature Communications, Vol. 10, 1055, 2019.

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

Harvard

Hansen, BK, Gupta, R, Baldus, L, Lyon, D, Narita, T, Lammers, M, Choudhary, C & Weinert, BT 2019, 'Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation', Nature Communications, vol. 10, 1055. https://doi.org/10.1038/s41467-019-09024-0

APA

Hansen, B. K., Gupta, R., Baldus, L., Lyon, D., Narita, T., Lammers, M., Choudhary, C., & Weinert, B. T. (2019). Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation. Nature Communications, 10, [1055]. https://doi.org/10.1038/s41467-019-09024-0

Vancouver

Hansen BK, Gupta R, Baldus L, Lyon D, Narita T, Lammers M et al. Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation. Nature Communications. 2019;10. 1055. https://doi.org/10.1038/s41467-019-09024-0

Author

Hansen, Bogi Karbech ; Gupta, Rajat ; Baldus, Linda ; Lyon, David ; Narita, Takeo ; Lammers, Michael ; Choudhary, Chunaram ; Weinert, Brian T. / Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation. In: Nature Communications. 2019 ; Vol. 10.

Bibtex

@article{06ac71a1adc34ec9896793902c5ebeea,
title = "Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation",
abstract = "Lysine acetylation is a reversible posttranslational modification that occurs at thousands of sites on human proteins. However, the stoichiometry of acetylation remains poorly characterized, and is important for understanding acetylation-dependent mechanisms of protein regulation. Here we provide accurate, validated measurements of acetylation stoichiometry at 6829 sites on 2535 proteins in human cervical cancer (HeLa) cells. Most acetylation occurs at very low stoichiometry (median 0.02%), whereas high stoichiometry acetylation (>1%) occurs on nuclear proteins involved in gene transcription and on acetyltransferases. Analysis of acetylation copy numbers show that histones harbor the majority of acetylated lysine residues in human cells. Class I deacetylases target a greater proportion of high stoichiometry acetylation compared to SIRT1 and HDAC6. The acetyltransferases CBP and p300 catalyze a majority (65%) of high stoichiometry acetylation. This resource dataset provides valuable information for evaluating the impact of individual acetylation sites on protein function and for building accurate mechanistic models.",
author = "Hansen, {Bogi Karbech} and Rajat Gupta and Linda Baldus and David Lyon and Takeo Narita and Michael Lammers and Chunaram Choudhary and Weinert, {Brian T.}",
year = "2019",
doi = "10.1038/s41467-019-09024-0",
language = "English",
volume = "10",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation

AU - Hansen, Bogi Karbech

AU - Gupta, Rajat

AU - Baldus, Linda

AU - Lyon, David

AU - Narita, Takeo

AU - Lammers, Michael

AU - Choudhary, Chunaram

AU - Weinert, Brian T.

PY - 2019

Y1 - 2019

N2 - Lysine acetylation is a reversible posttranslational modification that occurs at thousands of sites on human proteins. However, the stoichiometry of acetylation remains poorly characterized, and is important for understanding acetylation-dependent mechanisms of protein regulation. Here we provide accurate, validated measurements of acetylation stoichiometry at 6829 sites on 2535 proteins in human cervical cancer (HeLa) cells. Most acetylation occurs at very low stoichiometry (median 0.02%), whereas high stoichiometry acetylation (>1%) occurs on nuclear proteins involved in gene transcription and on acetyltransferases. Analysis of acetylation copy numbers show that histones harbor the majority of acetylated lysine residues in human cells. Class I deacetylases target a greater proportion of high stoichiometry acetylation compared to SIRT1 and HDAC6. The acetyltransferases CBP and p300 catalyze a majority (65%) of high stoichiometry acetylation. This resource dataset provides valuable information for evaluating the impact of individual acetylation sites on protein function and for building accurate mechanistic models.

AB - Lysine acetylation is a reversible posttranslational modification that occurs at thousands of sites on human proteins. However, the stoichiometry of acetylation remains poorly characterized, and is important for understanding acetylation-dependent mechanisms of protein regulation. Here we provide accurate, validated measurements of acetylation stoichiometry at 6829 sites on 2535 proteins in human cervical cancer (HeLa) cells. Most acetylation occurs at very low stoichiometry (median 0.02%), whereas high stoichiometry acetylation (>1%) occurs on nuclear proteins involved in gene transcription and on acetyltransferases. Analysis of acetylation copy numbers show that histones harbor the majority of acetylated lysine residues in human cells. Class I deacetylases target a greater proportion of high stoichiometry acetylation compared to SIRT1 and HDAC6. The acetyltransferases CBP and p300 catalyze a majority (65%) of high stoichiometry acetylation. This resource dataset provides valuable information for evaluating the impact of individual acetylation sites on protein function and for building accurate mechanistic models.

U2 - 10.1038/s41467-019-09024-0

DO - 10.1038/s41467-019-09024-0

M3 - Journal article

C2 - 30837475

VL - 10

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 1055

ER -

ID: 214462444