PXD052684 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | PUS7 cytoplasmic localization directs a pseudouridine-mediated cellular stress response |
| Description | Pseudouridine (Ψ) is an abundant post-transcriptional modification found across all classes of RNA. Since its discovery in mRNAs a decade ago, it has been widely speculated that Y might govern additional post-transcriptional regulation of gene expression. Here, we demonstrate that one of the principal enzymes responsible for adding Y to mRNAs, pseudouridine synthase 7 (PUS7), accumulates in the cytoplasm under a variety of stress conditions in Saccharomyces cerevisiae and BEAS-2B human epithelial lung cells. The localization of PUS7 to the cytoplasm promotes Y-incorporation into hundreds of different mRNA sequences and increases cellular fitness under ROS and divalent metal ion stress. The preponderance of newly identified Y-sites lies within portions of the mRNA important for post-transcriptional control—-coding regions and 3’ UTRs. Quantitative proteomics reveal that shifts in the cellular post-transcriptional modification landscape upon PUS7 relocalization reshapes the proteome. Our data suggest a mechanism whereby stressors localize PUS7 in the cytoplasm to enable the direct modification and regulation of stress response mRNAs, thereby protecting cells from further stress-induced damage.
(2A-PUS7-control 68283
2B-PUS7-control 68284
2C-PUS7-control 68285
4A-PUS7-NES-Co 68286
4A-PUS7-NES-Co 68287
4B-PUS7-NES-Co 68288
5A-PUS7-control-Co 68289
5B-PUS7-control-Co 68290
5C-PUS7-control-Co 68291
PUS7-NES_CU_1A 75059
PUS7-NES_CU_1B 75060
PUS7-NES_CU_1C 75061
PUS7-NLS_CU_2A 75062
PUS7-NLS_CU_2B 75063
PUS7-NLS_CU_2C 75064
PUS7-WT_CU_3A 75065
PUS7-WT_CU_3B 75066
PUS7-WT_CU_3C 75067) |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-01-28 |
| AnnouncementXML | Submission_2026-01-28_01:51:00.758.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Minli Ruan |
| SpeciesList | scientific name: Saccharomyces cerevisiae BY4741; NCBI TaxID: NEWT:1247190; |
| ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
| Instrument | Orbitrap Exploris 480 |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2024-05-29 14:30:23 | ID requested | |
| ⏵ 1 | 2026-01-28 01:51:01 | announced | |
Publication List
| Dataset with its publication pending |
Keyword List
Contact List
| Kristin Koutmou |
| contact affiliation | Associate Professor of Chemistry Dow Early Career Professor of Chemistry Associate Director of the Program in Chemical Biology Co-Director the Chemical Biology Interface Training Program University of Michigan 930 N University Ann Arbor, MI 48109 |
| contact email | kkoutmou@umich.edu |
| lab head | |
| Minli Ruan |
| contact affiliation | University of Michigan |
| contact email | mlruan@umich.edu |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
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| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD052684
- Label: PRIDE project
- Name: PUS7 cytoplasmic localization directs a pseudouridine-mediated cellular stress response