PXD028934 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Analysis of newly synthesized proteins more sensitive to Proteinase K using pulse SILAC and control sample for pulse SILAC experiment in which yeast cells were heat shock for 15 min and supernatant fractions analyzed (Experiment 1) |
Description | Accurate and efficient folding of nascent protein sequences into their native state requires support from the protein homeostasis network. Herein we probed which newly translated proteins are thermo-sensitive to infer which polypeptides require more time to fold within the proteome. Specifically, we determined which of these proteins were more susceptible to misfolding and aggregation under heat stress using pulse SILAC coupled mass spectrometry. These proteins are abundant, short, and highly structured. Notably these proteins display a tendency to form β-sheet secondary structures, a configuration which typically requires more time for folding, and were enriched for Hsp70/Ssb and TRiC/CCT binding motifs, suggesting a higher demand for chaperone-assisted folding. These polypeptides were also more often components of stable protein complexes in comparison to other proteins. Combining this evidence suggests that a specific subset of newly translated proteins in the cell requires more time following synthesis to reach a state less prone to aggregation upon stress. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_08:53:08.776.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Thibault Mayor |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | 6x(13)C labeled residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | impact II |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-10-04 10:02:51 | ID requested | |
1 | 2022-08-10 16:47:56 | announced | |
⏵ 2 | 2023-11-14 08:53:09 | announced | 2023-11-14: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: protein homeostasis, yeast,pulse SILAC, Limited Proteolysis |
Contact List
Thibault Mayor |
contact affiliation | The University of British Columbia |
contact email | mayor@mail.ubc.ca |
lab head | |
Thibault Mayor |
contact affiliation | University of British Columbia |
contact email | mayor@mail.ubc.ca |
dataset submitter | |
Full Dataset Link List
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/2022/08/PXD028934 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD028934
- Label: PRIDE project
- Name: Analysis of newly synthesized proteins more sensitive to Proteinase K using pulse SILAC and control sample for pulse SILAC experiment in which yeast cells were heat shock for 15 min and supernatant fractions analyzed (Experiment 1)