PXD003232

PXD003232 is an original dataset announced via ProteomeXchange.

Title	Identification of N-terminally arginylated proteins from the moss Physcomitrella patens
Description	Protein arginylation is a post-translational modification at the N-terminus of proteins and is crucial for viability and physiology in higher eukaryotes. The lack of arginylation causes severe developmental defects in plants and embryo lethality 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., 2015 New Phytol., DOI: 10.1111/nph.13656). Here we use a commercially available antibody against the fused reporter protein (GUS) to pull down ATE and its interacting proteins and validate the 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.
HostingRepository	PRIDE
AnnounceDate	2016-04-21
AnnouncementXML	Submission_2016-04-21_05:27:11.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD003232
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Ralf Reski
SpeciesList	scientific name: Physcomitrella patens subsp. patens (Moss); NCBI TaxID: 3218;
ModificationList	Ammonia-loss; Phospho; Oxidation; Acetyl; Carbamidomethyl; Gln->pyro-Glu
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2015-11-25 01:35:00	ID requested
⏵ 1	2016-04-21 05:27:12	announced

Hoernstein SN, Mueller SJ, Fiedler K, Schuelke M, Vanselow JT, Schuessele C, Lang D, Nitschke R, Igloi GL, Schlosser A, Reski R, Identification of Targets and Interaction Partners of Arginyl-tRNA Protein Transferase in the Moss Physcomitrella patens. Mol Cell Proteomics, 15(6):1808-22(2016) [pubmed]

curator keyword: Biological

submitter keyword: Physcomitrella patens, arginylation, N-end rule pathway

Ralf Reski
contact affiliation	Head, Chair Plant Biotechnology Faculty of Biology University of Freiburg Schaenzlestrasse 1 D-79104 Freiburg Germany
contact email	ralf.reski@biologie.uni-freiburg.de
lab head
Ralf Reski
contact affiliation	Faculty of Biology, University of Freiburg (Chair Plant Biotechnology), Schaenzlestr. 1, D-79104 Freiburg
contact email	ralf.reski@biologie.uni-freiburg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD003232
     1. Label: PRIDE project
     2. Name: Identification of N-terminally arginylated proteins from the moss Physcomitrella patens