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PXD014610

PXD014610 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleProteomic Analysis of Affinity-Purified Proteasomes Identifies a Suite of Assembly Chaperones in Arabidopsis
DescriptionThe 26S proteasome is an essential protease for the selective elimination of dysfunctional and short-lived regulatory proteins in eukaryotes. To define the composition of this multi-catalytic, ATP-dependent proteolytic machine in plants, we exploited Arabidopsis particles tagged at either the core protease (CP) or regulatory particle (RP) sub-complexes for rapid affinity purification followed by deep sequence analysis via mass spectrometry. Studies on proteasomes purified from whole seedlings via either a CP or RP subunit with or without ATP, which is needed to maintain the holo-proteasome complex, identified all known core subunits but failed to detect subunit isoform preferences, suggesting that Arabidopsis does not construct unique proteasomes sub-types. We also identified a suite of proteasome-interacting proteins, including likely orthologs of the yeast and mammalian chaperones Pba1, Pba2, Pba3, and Pba4 that assist in CP assembly; Ump1 that helps connect CP half-barrels; Nas2, Nas6, and Hsm3 that assist in RP assembly; and Ecm29 that promotes CP-RP association. Analysis of proteasomes enriched from seedlings exposed to the proteasome inhibitor MG132 revealed the accumulation of novel assembly intermediates, which reflect partially built proteasome sub-complexes associated with assembly chaperones, and the CP capped with the PA200/Blm10 regulator. Unlike in yeast, genetic analyses of Arabidopsis UMP1 showed that this chaperone is essential, with mutants missing the major UMP1a and UMP1b isoforms displaying a strong gametophytic defect. Single mutants impacting ump1a also accumulate a collection of proteasome assembly intermediates, consistent with its importance for CP construction. With this list of chaperones, it should now be possible to study the assembly events that generate the 26S holo-proteasome in Arabidopsis from the collection of 64 or more core subunits.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_04:04:59.087.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterDavid C Gemperline
SpeciesList scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationListubiquitination signature dipeptidyl lysine; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
InstrumentLTQ Orbitrap Velos; Q Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-07-15 02:45:37ID requested
12019-09-25 15:22:28announced
22019-11-08 00:40:58announced2019-11-08: Updated publication reference for PubMed record(s): 31562246.
32024-10-22 04:05:07announced2024-10-22: Updated project metadata.
Publication List
10.1074/jbc.ra119.010219;
Gemperline DC, Marshall RS, Lee KH, Zhao Q, Hu W, McLoughlin F, Scalf M, Smith LM, Vierstra RD, . J Biol Chem, 294(46):17570-17592(2019) [pubmed]
Keyword List
submitter keyword: chaperone
core protease
degradation
proteasome
proteolysis
regulatory particle
ubiquitin
Contact List
Richard D Vierstra
contact affiliationGeorge & Charmaine Mallinckrodt Professor Department of Biology Washington University in St. Louis
contact emailrdvierstra@wustl.edu
lab head
David C Gemperline
contact affiliationUW Madison
contact emaildcgemperline@gmail.com
dataset submitter
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Dataset FTP location
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