PXD003228-1

PXD003228 is an original dataset announced via ProteomeXchange.

Title	Interaction partners of arginyl-tRNA protein transferase in 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).
HostingRepository	PRIDE
AnnounceDate	2016-04-19
AnnouncementXML	Submission_2016-04-19_02:59:11.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jens Vanselow
SpeciesList	scientific name: Physcomitrella patens subsp. patens (Moss); NCBI TaxID: 3218;
ModificationList	No PTMs are included in the dataset
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2015-11-23 23:46:08	ID requested
⏵ 1	2016-04-19 02:59:12	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: moss, Physcomitrella patens, LC-MS/MS, protein interaction, co-IP

Andreas Schlosser
contact affiliation	Rudolf-Virchow-Zentrum for Experimental Biomedicine, University of Würzburg, Josef-Schneider-Str. 2, 97080 Würzburg, Germany
contact email	andreas.schlosser@virchow.uni-wuerzburg.de
lab head
Jens Vanselow
contact affiliation	University Wuerzburg
contact email	jens.vanselow@uni-wuerzburg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2016/04/PXD003228

PRIDE project URI

• PRIDE
  1. PXD003228
     1. Label: PRIDE project
     2. Name: Interaction partners of arginyl-tRNA protein transferase in the moss Physcomitrella patens