PXD044481 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Macromolecular condensation buffers intracellular water potential |
| Description | Optimum protein function and biochemical activity critically depends on water availability, because solvent thermodynamics drive protein folding and macromolecular interactions. Reciprocally, macromolecules restrict the movement of “structured” water molecules within their hydration layers, reducing the available “free” bulk solvent and therefore the total thermodynamic potential energy of water, or water potential. Within concentrated macromolecular solutions like the cytosol, we found modest changes in temperature greatly impact the water potential, and are counteracted by opposing changes in osmotic strength. Remarkably, this duality of temperature and osmotic strength allows simple manipulations of solvent thermodynamics to prevent cell death upon extreme cold or heat shock. Physiologically, cells must sustain their activity against fluctuating temperature, pressure and osmotic strength that impact water availability within seconds. Yet, established mechanisms of water homeostasis act over much slower timescales, so we postulated the existence of a rapid compensatory response. We find this function is performed by water potential-driven changes in macromolecular assembly, particularly biomolecular condensation of intrinsically-disordered proteins. Formation or dissolution of biomolecular condensates liberates and captures free water, respectively, quickly counteracting thermal or osmotic perturbations of water potential, which in consequence is robustly buffered in the cytoplasm. Our results indicate biomolecular condensation constitutes an intrinsic biophysical feedback response that rapidly compensates for intracellular osmotic and thermal fluctuations. We suggest preserving water availability within the concentrated cytosol is an overlooked evolutionary driver of protein (dis)order and function. |
| HostingRepository | PRIDE |
| AnnounceDate | 2024-10-22 |
| AnnouncementXML | Submission_2024-10-22_06:03:40.467.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Sew Peak-Chew |
| SpeciesList | scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; |
| ModificationList | phosphorylated residue |
| Instrument | Q Exactive |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|
| 0 | 2023-08-10 08:13:02 | ID requested | |
| 1 | 2023-09-22 02:39:45 | announced | |
| 2 | 2023-11-14 07:47:28 | announced | 2023-11-14: Updated project metadata. |
| ⏵ 3 | 2024-10-22 06:03:40 | announced | 2024-10-22: Updated project metadata. |
Publication List
Keyword List
| submitter keyword: membraneless organelles,phase separation, water potential |
Contact List
| John S. O'Neill |
|---|
| contact affiliation | MRC Laboratory of Molecular Biology, Francis Crick Avenue,Cambridge, UK |
| contact email | oneillj@mrc-lmb.cam.ac.uk |
| lab head | |
| Sew Peak-Chew |
|---|
| contact affiliation | MRC-LMB |
| contact email | spc@mrc-lmb.cam.ac.uk |
| 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/2023/09/PXD044481 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD044481
- Label: PRIDE project
- Name: Macromolecular condensation buffers intracellular water potential
to receive all new ProteomeXchange dataset release announcements!
