Cotranslational N-degron masking by acetylation promotes proteome stability in plants

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Standard

Cotranslational N-degron masking by acetylation promotes proteome stability in plants. / Linster, Eric; Forero Ruiz, Francy L; Miklankova, Pavlina; Ruppert, Thomas; Mueller, Johannes; Armbruster, Laura; Gong, Xiaodi; Serino, Giovanna; Mann, Matthias; Hell, Rüdiger; Wirtz, Markus.

In: Nature Communications, Vol. 13, No. 1, 2022, p. 810.

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

Harvard

Linster, E, Forero Ruiz, FL, Miklankova, P, Ruppert, T, Mueller, J, Armbruster, L, Gong, X, Serino, G, Mann, M, Hell, R & Wirtz, M 2022, 'Cotranslational N-degron masking by acetylation promotes proteome stability in plants', Nature Communications, vol. 13, no. 1, pp. 810. https://doi.org/10.1038/s41467-022-28414-5

APA

Linster, E., Forero Ruiz, F. L., Miklankova, P., Ruppert, T., Mueller, J., Armbruster, L., Gong, X., Serino, G., Mann, M., Hell, R., & Wirtz, M. (2022). Cotranslational N-degron masking by acetylation promotes proteome stability in plants. Nature Communications, 13(1), 810. https://doi.org/10.1038/s41467-022-28414-5

Vancouver

Linster E, Forero Ruiz FL, Miklankova P, Ruppert T, Mueller J, Armbruster L et al. Cotranslational N-degron masking by acetylation promotes proteome stability in plants. Nature Communications. 2022;13(1):810. https://doi.org/10.1038/s41467-022-28414-5

Author

Linster, Eric ; Forero Ruiz, Francy L ; Miklankova, Pavlina ; Ruppert, Thomas ; Mueller, Johannes ; Armbruster, Laura ; Gong, Xiaodi ; Serino, Giovanna ; Mann, Matthias ; Hell, Rüdiger ; Wirtz, Markus. / Cotranslational N-degron masking by acetylation promotes proteome stability in plants. In: Nature Communications. 2022 ; Vol. 13, No. 1. pp. 810.

Bibtex

@article{57410febbc9940d0adf2695da2050629,
title = "Cotranslational N-degron masking by acetylation promotes proteome stability in plants",
abstract = "N-terminal protein acetylation (NTA) is a prevalent protein modification essential for viability in animals and plants. The dominant executor of NTA is the ribosome tethered Nα-acetyltransferase A (NatA) complex. However, the impact of NatA on protein fate is still enigmatic. Here, we demonstrate that depletion of NatA activity leads to a 4-fold increase in global protein turnover via the ubiquitin-proteasome system in Arabidopsis. Surprisingly, a concomitant increase in translation, actioned via enhanced Target-of-Rapamycin activity, is also observed, implying that defective NTA triggers feedback mechanisms to maintain steady-state protein abundance. Quantitative analysis of the proteome, the translatome, and the ubiquitome reveals that NatA substrates account for the bulk of this enhanced turnover. A targeted analysis of NatA substrate stability uncovers that NTA absence triggers protein destabilization via a previously undescribed and widely conserved nonAc/N-degron in plants. Hence, the imprinting of the proteome with acetylation marks is essential for coordinating proteome stability.",
author = "Eric Linster and {Forero Ruiz}, {Francy L} and Pavlina Miklankova and Thomas Ruppert and Johannes Mueller and Laura Armbruster and Xiaodi Gong and Giovanna Serino and Matthias Mann and R{\"u}diger Hell and Markus Wirtz",
note = "{\textcopyright} 2022. The Author(s).",
year = "2022",
doi = "10.1038/s41467-022-28414-5",
language = "English",
volume = "13",
pages = "810",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Cotranslational N-degron masking by acetylation promotes proteome stability in plants

AU - Linster, Eric

AU - Forero Ruiz, Francy L

AU - Miklankova, Pavlina

AU - Ruppert, Thomas

AU - Mueller, Johannes

AU - Armbruster, Laura

AU - Gong, Xiaodi

AU - Serino, Giovanna

AU - Mann, Matthias

AU - Hell, Rüdiger

AU - Wirtz, Markus

N1 - © 2022. The Author(s).

PY - 2022

Y1 - 2022

N2 - N-terminal protein acetylation (NTA) is a prevalent protein modification essential for viability in animals and plants. The dominant executor of NTA is the ribosome tethered Nα-acetyltransferase A (NatA) complex. However, the impact of NatA on protein fate is still enigmatic. Here, we demonstrate that depletion of NatA activity leads to a 4-fold increase in global protein turnover via the ubiquitin-proteasome system in Arabidopsis. Surprisingly, a concomitant increase in translation, actioned via enhanced Target-of-Rapamycin activity, is also observed, implying that defective NTA triggers feedback mechanisms to maintain steady-state protein abundance. Quantitative analysis of the proteome, the translatome, and the ubiquitome reveals that NatA substrates account for the bulk of this enhanced turnover. A targeted analysis of NatA substrate stability uncovers that NTA absence triggers protein destabilization via a previously undescribed and widely conserved nonAc/N-degron in plants. Hence, the imprinting of the proteome with acetylation marks is essential for coordinating proteome stability.

AB - N-terminal protein acetylation (NTA) is a prevalent protein modification essential for viability in animals and plants. The dominant executor of NTA is the ribosome tethered Nα-acetyltransferase A (NatA) complex. However, the impact of NatA on protein fate is still enigmatic. Here, we demonstrate that depletion of NatA activity leads to a 4-fold increase in global protein turnover via the ubiquitin-proteasome system in Arabidopsis. Surprisingly, a concomitant increase in translation, actioned via enhanced Target-of-Rapamycin activity, is also observed, implying that defective NTA triggers feedback mechanisms to maintain steady-state protein abundance. Quantitative analysis of the proteome, the translatome, and the ubiquitome reveals that NatA substrates account for the bulk of this enhanced turnover. A targeted analysis of NatA substrate stability uncovers that NTA absence triggers protein destabilization via a previously undescribed and widely conserved nonAc/N-degron in plants. Hence, the imprinting of the proteome with acetylation marks is essential for coordinating proteome stability.

U2 - 10.1038/s41467-022-28414-5

DO - 10.1038/s41467-022-28414-5

M3 - Journal article

C2 - 35145090

VL - 13

SP - 810

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

ER -

ID: 292144066