ArticleMolecular & cellular proteomics : MCP2016
Identification of Targets and Interaction Partners of Arginyl-tRNA Protein Transferase in the Moss Physcomitrella patens.
Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 35 citations in OpenAlex.
- Implementing N-terminomics and machine learning to probe Nt-arginylation.Nature communications · 2025Article
- Acylamino acid-releasing enzyme, a bifunctional protease with a potential role in aging.Journal of experimental botany · 2025Review
- A FLOE-related protein regulates the two-dimensional to three-dimensional growth transition in the moss Physcomitrium patens.Development (Cambridge, England) · 2025Article
- Recombinant production of spider silk protein in Physcomitrella photobioreactors.Plant cell reports · 2025Article
- A snapshot of the Physcomitrella N-terminome reveals N-terminal methylation of organellar proteins.Plant cell reports · 2024Article
- A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis.Communications biology · 2023Article
- ATE1-Mediated Post-Translational Arginylation Is an Essential Regulator of Eukaryotic Cellular Homeostasis.ACS chemical biology · 2020Article
- Challenges ofPlant signaling & behavior · 2020Article
- New beginnings and new ends: methods for large-scale characterization of protein termini and their use in plant biology.Journal of experimental botany · 2019Review
- Target site specificity and in vivo complexity of the mammalian arginylome.Scientific reports · 2018Article
- The single berberine bridge enzyme homolog of Physcomitrella patens is a cellobiose oxidase.The FEBS journal · 2018Article
- Real-time detection of N-end rule-mediated ubiquitination via fluorescently labeled substrate probes.The New phytologist · 2018Article
- Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets.Nature communications · 2017Article
- Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein arginylation is a posttranslational modification of both N-terminal amino acids of proteins and sidechain carboxylates and can be crucial for viability and physiology in higher eukaryotes. The lack of arginylation causes severe developmental defects in moss, affects the low oxygen response in Arabidopsis thaliana and is embryo lethal in Drosophila and in mice. Although several studies investigated impact and function of the responsible enzyme, the arginyl-tRNA protein transferase (ATE) in plants, identification of arginylated proteins by mass spectrometry was not hitherto achieved. In the present study, we report the identification of targets and interaction partners of ATE in the model plant Physcomitrella patens by mass spectrometry, employing two different immuno-affinity strategies and a recently established transgenic ATE:GUS reporter line (Schuessele et al., 2016 New Phytol. , DOI: 10.1111/nph.13656). Here we use a commercially available antibody against the fused reporter protein (β-glucuronidase) to pull down ATE and its interacting proteins and validate its in vivo interaction with a class I small heatshock protein via Förster resonance energy transfer (FRET). Additionally, we apply and modify a method that already successfully identified arginylated proteins from mouse proteomes by using custom-made antibodies specific for N-terminal arginine. As a result, we identify four arginylated proteins from Physcomitrella patens with high confidence.Data are available via ProteomeXchange with identifier PXD003228 and PXD003232.
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