PXD044216 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Proteome analysis of ROF-FKBP mutants reveals functional relations between heat stress responses, plant development and protein quality control during heat acclimation in A. thaliana |
Description | In the present study, a differential screening following heat stress acclimation was performed in A. thaliana WT and ROF-FKBP mutated plants, using mass spectrometry, and the results were used to understand and analyze the effect of the ROF PPIases during thermotolerance acquisition in plants. Our data highlight the central role of these two PPIases in heat stress and point to their direct or indirect effect on other proteins participating in cellular functions such as protein folding and quality control, cell division, photosynthesis, and other metabolic and signaling processes. 1) Specifically, the heat stress response, protein folding and protein ER processing pathways are enhanced following a 37 oC acclimation period independently to the mutation state. 2) However, at 37 oC and in the double mutated rof1–/2 –plants, a higher accumulation of proteins belonging to the above pathways is observed compared to all other conditions (WT, mutants, control and heat stressed). 3) Furthermore, the proteasomal pathway including the common member of both the protasomal and lysosomal degradation pathway CDC48, is over-represented in the extracts of both untreated and heat stressed rof1–/2 – mutants compared to the other extracts. 4) In contrast, in the single rof1 – mutation the heat acclimation (including ROF2), protein folding and proteasomal pathways are significantly suppressed compared to the WT, at 37 oC. 5) Protein accumulation related to the heat stress and protein quality control pathways follow the rof1–/2 – > rof2 – > rof1 – pattern suggesting a differential but also synergistic role of the two proteins. 6) Protein complexes of other biochemical pathways such as the Lhc of the photosynthetic pathway and the phosphoinositide binding proteins involved in membrane-trafficking events during cell plate formation and cytokinesis (Patellin-1, 2 and 3) are negatively regulated by the rof1–/2 – mutants. Our results suggest that ROF1 and ROF2 FKBPs regulate stress response, developmental and metabolic pathways via a complex feedback mechanism that ensures the continuation of protein quality control at their absence. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_06:25:44.175.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Martina Samiotaki |
SpeciesList | scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; |
ModificationList | monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap XL |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-07-31 04:26:28 | ID requested | |
1 | 2024-01-26 06:53:37 | announced | |
⏵ 2 | 2024-10-22 06:25:50 | announced | 2024-10-22: Updated project metadata. |
Publication List
Keyword List
submitter keyword: ROF2, FKBP, heat, stress, Protein quality control, HSPs, Patellin, proteasome, plant, quantitative proteomics, CDC48,ROF1 |
Contact List
Theodora Farmaki |
contact affiliation | Institute of Applied Biosciences, Center for Research and Technology - Hellas, 6th km Charilaou - Thermi rd. 570 01 Thermi Thessaloniki |
contact email | mfarmaki@certh.gr |
lab head | |
Martina Samiotaki |
contact affiliation | Protein Analysis Laboratory B.S.R.C. "Alexander Fleming", Alexander Fleming Street 34 16672, Vari, Greece |
contact email | samiotaki@fleming.gr |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD044216
- Label: PRIDE project
- Name: Proteome analysis of ROF-FKBP mutants reveals functional relations between heat stress responses, plant development and protein quality control during heat acclimation in A. thaliana