Dataset Information

Quantification of poly-ubiquitinated proteins in wild type Arabidopsis and amiNAA10 plants

ABSTRACT: Wild type Arabidopsis Col-0 plants and mutants depleted of the catalytic subunit of the ribosome-associated N-acetyltransferase A (NatA) complex (amiNAA10) were grown on soil for six weeks under short-day conditions (8h light, light intensity: 100 µE, 21 °C/18 °C temperature (day/night), 50 % humidity). Proteasome and deubiquitinase activity were inhibited at 10 am (2 h of light) by floating leaf discs on ½ Hoagland supplemented with 50 µM MG132 and 20 µM PR-619 for 5 h.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Thomas Ruppert

LAB HEAD: Thomas Ruppert

PROVIDER: PXD024329 | Pride | 2022-04-04

REPOSITORIES: Pride

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Publications

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

Linster Eric E Forero Ruiz Francy L FL Miklankova Pavlina P Ruppert Thomas T Mueller Johannes J Armbruster Laura L Gong Xiaodi X Serino Giovanna G Mann Matthias M Hell Rüdiger R Wirtz Markus M

Nature communications 20220210 1

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 N<sup>α</sup>-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, ...[more]

PMID: 35145090

Dataset Information

Quantification of poly-ubiquitinated proteins in wild type Arabidopsis and amiNAA10 plants

Publications

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

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