Proteomics

Dataset Information

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Quantification of the translatome 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). The translatome of both genotypes after 2 hours of light (10 am) was determined by feeding of the trackable Met-analogue azidohomoalanine for 4 hours to leaf disks floated on ½ Hoagland medium containing 50 µM azidohomoalanine in the light.

INSTRUMENT(S): Q Exactive

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

TISSUE(S): Leaf

SUBMITTER: Thomas Ruppert  

LAB HEAD: Thomas Ruppert

PROVIDER: PXD024328 | Pride | 2022-04-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
18-229_proteinGroups.txt Txt
QE25D060-18-229-01.raw Raw
QE25D060-18-229-02.raw Raw
QE25D060-18-229-03.raw Raw
QE25D060-18-229-04.raw Raw
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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]

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