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PXD033843

PXD033843 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleDuplicated ribosomal protein paralogs promote alternative translation and drug resistance
DescriptionRibosomes are often seen as monolithic machines produced from uniformly regulated genes. However, in yeast most ribosomal proteins come from duplicated genes. Here, we demonstrate that gene duplication may serve as a stress-adaptation mechanism modulating the global proteome through the differential expression of ribosomal protein paralogs. Our data indicate that the yeast paralog pair of the ribosomal protein L7/uL30 produces two differentially acetylated proteins. Under normal conditions most ribosomes incorporate the hypo-acetylated major form favoring the translation of genes with short open reading frames. Exposure to drugs, on the other hand, increases the production of ribosomes carrying the hyper-acetylated minor paralog that increases translation of long open reading frames. Many of these paralogs dependent genes encode cell wall proteins that could promote tolerance to drugs as their translation increases after exposure to drugs. Together the data reveal a mechanism of translation control through the differential use of near-identical ribosomal protein isoforms.
HostingRepositoryPRIDE
AnnounceDate2022-08-09
AnnouncementXMLSubmission_2022-08-09_11:50:42.301.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterMathieu Catala
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListcarbamoylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-05-12 04:29:44ID requested
12022-08-09 11:50:42announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: Saccharomyces cerevisiae, dRPG, paralogs
Contact List
Sherif Abou Elela
contact affiliationUniversite de Sherbrooke
contact emailsherif.abou.elela@usherbrooke.ca
lab head
Mathieu Catala
contact affiliationUniversite de Sherbrooke
contact emailmathieu.catala@usherbrooke.ca
dataset submitter
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