Protein modifications and ionic strength show the difference between protein-mediated and solvent-mediated regulation of biomolecular condensation
Biomolecular condensation is an important mechanism of cellular compartmentalization without membranes. Formation of liquid-like condensates of biomolecules involves protein-protein interactions working in tandem with protein-water interactions. The balance of these interactions in condensate-formin...
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Frontiers Media S.A.
2025-03-01
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| Series: | Frontiers in Nanotechnology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fnano.2025.1556384/full |
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| author | Artur Czajkowski Artur Czajkowski Abhirami Udayabanu Abhirami Udayabanu Manthan Raj Manthan Raj Likhitha Ch. P. Pulibandla Likhitha Ch. P. Pulibandla Marija Tursunović Marcus Jahnel Marcus Jahnel Ellen M. Adams Ellen M. Adams |
| author_facet | Artur Czajkowski Artur Czajkowski Abhirami Udayabanu Abhirami Udayabanu Manthan Raj Manthan Raj Likhitha Ch. P. Pulibandla Likhitha Ch. P. Pulibandla Marija Tursunović Marcus Jahnel Marcus Jahnel Ellen M. Adams Ellen M. Adams |
| author_sort | Artur Czajkowski |
| collection | DOAJ |
| description | Biomolecular condensation is an important mechanism of cellular compartmentalization without membranes. Formation of liquid-like condensates of biomolecules involves protein-protein interactions working in tandem with protein-water interactions. The balance of these interactions in condensate-forming proteins is impacted by multiple factors inside of a living organism. This work investigates the effects of post-translational modifications (PTMs) and salt concentration as two such perturbing factors on the protein Fused in Sarcoma (FUS), an RNA binding protein. The protein was obtained from two expression systems differing by their capability to add PTMs to the protein, bacterial and insect cell. Attenuated total reflection Terahertz spectroscopy is used to probe the solvation behavior in condensates formed from FUS protein with and without PTMs at 100 mM and 2.5 M KCl. The results show that while PTMs impact the phase-separating propensity, they do not alter protein solvation in the condensate. On the other hand, salt concentration was found to alter the stiffness of the water hydrogen bond network. These findings have implications for biomolecular condensates chemistry, showing that condensate molecular organization is perturbed by fluctuations in solvent properties. |
| format | Article |
| id | doaj-art-711167b4bdef48fa8cf0d400fca9c9a2 |
| institution | OA Journals |
| issn | 2673-3013 |
| language | English |
| publishDate | 2025-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Nanotechnology |
| spelling | doaj-art-711167b4bdef48fa8cf0d400fca9c9a22025-08-20T02:03:07ZengFrontiers Media S.A.Frontiers in Nanotechnology2673-30132025-03-01710.3389/fnano.2025.15563841556384Protein modifications and ionic strength show the difference between protein-mediated and solvent-mediated regulation of biomolecular condensationArtur Czajkowski0Artur Czajkowski1Abhirami Udayabanu2Abhirami Udayabanu3Manthan Raj4Manthan Raj5Likhitha Ch. P. Pulibandla6Likhitha Ch. P. Pulibandla7Marija Tursunović8Marcus Jahnel9Marcus Jahnel10Ellen M. Adams11Ellen M. Adams12Cluster of Excellence Physics of Life, TU Dresden, Dresden, GermanyInstitute of Resource Ecology, Helmholtz Zentrum Dresden Rossendorf, Dresden, GermanyCluster of Excellence Physics of Life, TU Dresden, Dresden, GermanyInstitute of Resource Ecology, Helmholtz Zentrum Dresden Rossendorf, Dresden, GermanyCluster of Excellence Physics of Life, TU Dresden, Dresden, GermanyInstitute of Resource Ecology, Helmholtz Zentrum Dresden Rossendorf, Dresden, GermanyCluster of Excellence Physics of Life, TU Dresden, Dresden, GermanyInstitute of Resource Ecology, Helmholtz Zentrum Dresden Rossendorf, Dresden, GermanyFaculty of Chemistry, University of Belgrade, Belgrade, SerbiaCluster of Excellence Physics of Life, TU Dresden, Dresden, GermanyBiotechnology Center (BIOTEC), Center for Molecular and Cellular Bioengineering (CMCB), TU Dresden, Dresden, GermanyCluster of Excellence Physics of Life, TU Dresden, Dresden, GermanyInstitute of Resource Ecology, Helmholtz Zentrum Dresden Rossendorf, Dresden, GermanyBiomolecular condensation is an important mechanism of cellular compartmentalization without membranes. Formation of liquid-like condensates of biomolecules involves protein-protein interactions working in tandem with protein-water interactions. The balance of these interactions in condensate-forming proteins is impacted by multiple factors inside of a living organism. This work investigates the effects of post-translational modifications (PTMs) and salt concentration as two such perturbing factors on the protein Fused in Sarcoma (FUS), an RNA binding protein. The protein was obtained from two expression systems differing by their capability to add PTMs to the protein, bacterial and insect cell. Attenuated total reflection Terahertz spectroscopy is used to probe the solvation behavior in condensates formed from FUS protein with and without PTMs at 100 mM and 2.5 M KCl. The results show that while PTMs impact the phase-separating propensity, they do not alter protein solvation in the condensate. On the other hand, salt concentration was found to alter the stiffness of the water hydrogen bond network. These findings have implications for biomolecular condensates chemistry, showing that condensate molecular organization is perturbed by fluctuations in solvent properties.https://www.frontiersin.org/articles/10.3389/fnano.2025.1556384/fullbiomolecular condensatesprotein solvationTHz spectroscopyreentrant phase separationpost-translational modifications |
| spellingShingle | Artur Czajkowski Artur Czajkowski Abhirami Udayabanu Abhirami Udayabanu Manthan Raj Manthan Raj Likhitha Ch. P. Pulibandla Likhitha Ch. P. Pulibandla Marija Tursunović Marcus Jahnel Marcus Jahnel Ellen M. Adams Ellen M. Adams Protein modifications and ionic strength show the difference between protein-mediated and solvent-mediated regulation of biomolecular condensation Frontiers in Nanotechnology biomolecular condensates protein solvation THz spectroscopy reentrant phase separation post-translational modifications |
| title | Protein modifications and ionic strength show the difference between protein-mediated and solvent-mediated regulation of biomolecular condensation |
| title_full | Protein modifications and ionic strength show the difference between protein-mediated and solvent-mediated regulation of biomolecular condensation |
| title_fullStr | Protein modifications and ionic strength show the difference between protein-mediated and solvent-mediated regulation of biomolecular condensation |
| title_full_unstemmed | Protein modifications and ionic strength show the difference between protein-mediated and solvent-mediated regulation of biomolecular condensation |
| title_short | Protein modifications and ionic strength show the difference between protein-mediated and solvent-mediated regulation of biomolecular condensation |
| title_sort | protein modifications and ionic strength show the difference between protein mediated and solvent mediated regulation of biomolecular condensation |
| topic | biomolecular condensates protein solvation THz spectroscopy reentrant phase separation post-translational modifications |
| url | https://www.frontiersin.org/articles/10.3389/fnano.2025.1556384/full |
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