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PXD033057

PXD033057 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleTwo aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein
DescriptionAminoacyl-tRNA synthetases (aaRSs) attach amino acids to their cognate transfer RNAs. In eukaryotes, a subset of cytosolic aaRSs is organized into a multi-synthetase complex (MSC), along with specialized scaffolding proteins referred to as aaRS-interacting multifunctional proteins (AIMPs). In Plasmodium, the causative agent of malaria, the tRNA import protein (tRip), is a membrane protein which participates in tRNA trafficking. Here, we show that tRip is also an AIMP. We identified three aaRSs, namely the glutamyl- (ERS), glutaminyl- (QRS), and methionyl- (MRS) tRNA synthetases, which were specifically co-immunoprecipitated with tRip in Plasmodium berghei blood stage parasites. All four proteins contain an N-terminal GST-like domain involved in MSC assembly. Surprisingly, further dissection of GST-like interactions identified two exclusive heterotrimeric complexes: Q-complex (tRip:ERS:QRS) and M-complex (tRip:ERS:MRS). Gel filtration and light scattering suggest a 2:2:2 stoichiometry for both complexes but with distinct biophysical properties and mutational analysis revealed that the GST-like domains of QRS and MRS use different strategies to bind ERS. Furthermore, the modular organization of the assembled aaRSs and the properties of the specific additional modules supported the proposed localization of these complexes at the parasite membrane.
HostingRepositoryPRIDE
AnnounceDate2022-06-09
AnnouncementXMLSubmission_2022-06-09_10:22:18.272.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD033057
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterJohana Chicher
SpeciesList scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListacetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentTripleTOF 5600; Q Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-04-07 03:11:57ID requested
12022-06-09 10:22:19announced
Publication List
Jaramillo Ponce JR, Kapps D, Paulus C, Chicher J, Frugier M, Discovery of two distinct aminoacyl-tRNA synthetase complexes anchored to the Plasmodium surface tRNA import protein. J Biol Chem, 298(6):101987(2022) [pubmed]
Keyword List
submitter keyword: aminoacyl-tRNA synthetase, tRNA, RNA binding protein, protein complex, Cell surface protein Multi-aminoacyl-tRNA synthetase complex (MARS/MSC), GST-like domain, aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMP)
Contact List
Magali Frugier
contact affiliationUniversité de Strasbourg, CNRS, Architecture et Réactivité de l’ARN, UPR 9002, F-67084 Strasbourg, France
contact emailm.frugier@ibmc-cnrs.unistra.fr
lab head
Johana Chicher
contact affiliationUniversité de Strasbourg, Plateforme Protéomique Strasbourg-Esplanade, Centre National de la Recherche Scientifique
contact emailj.chicher@ibmc-cnrs.unistra.fr
dataset submitter
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