Macromolecular condensation buffers intracellular water potential

Optimum protein function and biochemical activity critically depends on water availability because solvent thermodynamics drive protein folding and macromolecular interactions 1 . Reciprocally, macromolecules restrict the movement of ‘structured’ water molecules within their hydration layers, reduci...

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Published inNature (London) Vol. 623; no. 7988; pp. 842 - 852
Main Authors Watson, Joseph L., Seinkmane, Estere, Styles, Christine T., Mihut, Andrei, Krüger, Lara K., McNally, Kerrie E., Planelles-Herrero, Vicente Jose, Dudek, Michal, McCall, Patrick M., Barbiero, Silvia, Vanden Oever, Michael, Peak-Chew, Sew Yeu, Porebski, Benjamin T., Zeng, Aiwei, Rzechorzek, Nina M., Wong, David C. S., Beale, Andrew D., Stangherlin, Alessandra, Riggi, Margot, Iwasa, Janet, Morf, Jörg, Miliotis, Christos, Guna, Alina, Inglis, Alison J., Brugués, Jan, Voorhees, Rebecca M., Chambers, Joseph E., Meng, Qing-Jun, O’Neill, John S., Edgar, Rachel S., Derivery, Emmanuel
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 23.11.2023
Nature Publishing Group
Subjects
13
13/62
14
14/19
631/45/470
631/57/2269
631/80
631/80/458
Cell Death
Cytosol - chemistry
Cytosol - metabolism
Denaturation
Homeostasis
Humanities and Social Sciences
Hydration
Hydrogen
Intracellular
Kinases
Low temperature
Macromolecular Substances - chemistry
Macromolecular Substances - metabolism
Macromolecules
Molecular dynamics
multidisciplinary
Osmolar Concentration
Pressure
Protein denaturation
Protein folding
Proteins
Proteins - chemistry
Proteins - metabolism
Science
Science (multidisciplinary)
Solvents
Solvents - chemistry
Solvents - metabolism
Temperature
Temperature dependence
Thermodynamics
Time Factors
Water - chemistry
Water - metabolism
Water availability
Water content
Water potential
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Abstract Optimum protein function and biochemical activity critically depends on water availability because solvent thermodynamics drive protein folding and macromolecular interactions 1 . 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. Here, within concentrated macromolecular solutions such as the cytosol, we found that modest changes in temperature greatly affect the water potential, and are counteracted by opposing changes in osmotic strength. This duality of temperature and osmotic strength enables simple manipulations of solvent thermodynamics to prevent cell death after extreme cold or heat shock. Physiologically, cells must sustain their activity against fluctuating temperature, pressure and osmotic strength, which impact water availability within seconds. Yet, established mechanisms of water homeostasis act over much slower timescales 2 , 3 ; we therefore postulated the existence of a rapid compensatory response. We find that this function is performed by water potential-driven changes in macromolecular assembly, particularly biomolecular condensation of intrinsically disordered proteins. The formation and dissolution of biomolecular condensates liberates and captures free water, respectively, quickly counteracting thermal or osmotic perturbations of water potential, which is consequently robustly buffered in the cytoplasm. Our results indicate that biomolecular condensation constitutes an intrinsic biophysical feedback response that rapidly compensates for intracellular osmotic and thermal fluctuations. We suggest that preserving water availability within the concentrated cytosol is an overlooked evolutionary driver of protein (dis)order and function. Water thermodynamics drive changes in macromolecular assembly that rapidly restore intracellular water availability in response to physiological fluctuations in temperature, pressure and osmotic strength.
AbstractList Optimum protein function and biochemical activity critically depends on water availability because solvent thermodynamics drive protein folding and macromolecular interactions 1 . 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. Here, within concentrated macromolecular solutions such as the cytosol, we found that modest changes in temperature greatly affect the water potential, and are counteracted by opposing changes in osmotic strength. This duality of temperature and osmotic strength enables simple manipulations of solvent thermodynamics to prevent cell death after extreme cold or heat shock. Physiologically, cells must sustain their activity against fluctuating temperature, pressure and osmotic strength, which impact water availability within seconds. Yet, established mechanisms of water homeostasis act over much slower timescales 2 , 3 ; we therefore postulated the existence of a rapid compensatory response. We find that this function is performed by water potential-driven changes in macromolecular assembly, particularly biomolecular condensation of intrinsically disordered proteins. The formation and dissolution of biomolecular condensates liberates and captures free water, respectively, quickly counteracting thermal or osmotic perturbations of water potential, which is consequently robustly buffered in the cytoplasm. Our results indicate that biomolecular condensation constitutes an intrinsic biophysical feedback response that rapidly compensates for intracellular osmotic and thermal fluctuations. We suggest that preserving water availability within the concentrated cytosol is an overlooked evolutionary driver of protein (dis)order and function. Water thermodynamics drive changes in macromolecular assembly that rapidly restore intracellular water availability in response to physiological fluctuations in temperature, pressure and osmotic strength.
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. Here, within concentrated macromolecular solutions such as the cytosol, we found that modest changes in temperature greatly affect the water potential, and are counteracted by opposing changes in osmotic strength. This duality of temperature and osmotic strength enables simple manipulations of solvent thermodynamics to prevent cell death after extreme cold or heat shock. Physiologically, cells must sustain their activity against fluctuating temperature, pressure and osmotic strength, which impact water availability within seconds. Yet, established mechanisms of water homeostasis act over much slower timescales ; we therefore postulated the existence of a rapid compensatory response. We find that this function is performed by water potential-driven changes in macromolecular assembly, particularly biomolecular condensation of intrinsically disordered proteins. The formation and dissolution of biomolecular condensates liberates and captures free water, respectively, quickly counteracting thermal or osmotic perturbations of water potential, which is consequently robustly buffered in the cytoplasm. Our results indicate that biomolecular condensation constitutes an intrinsic biophysical feedback response that rapidly compensates for intracellular osmotic and thermal fluctuations. We suggest that preserving water availability within the concentrated cytosol is an overlooked evolutionary driver of protein (dis)order and function.
In other words, water is required to hydrate macromolecules and make them fold properly, but this restricts the movement of water molecules and thereby diminishes their availability. [...]cells must maintain water availability within an optimal range for protein activity, biochemical efficiency and, ultimately, viability. Molecular dynamics simulations and studies of protein cold denaturation have both previously suggested that increased macromolecular hydration occurs at lower temperatures and is also consistent with temperature-dependent changes in linear alcohol hydration11 " . From our observations in solution, we predicted that intracellular water potential would be similarly sensitive to acute changes in macromolecular hydration elicited by perturbation of temperature and extracellular osmotic strength, because both affect the ratio of free to structured water (Fig. lb). Using Fluo-4 imaging, we confirmed that acute hyperosmotic treatment evoked a dose-dependent increase in Ca2+signallingand validated our prediction that an acute temperature decrease would evoke a similar response, whereas hypoosmotic treatment had no effect (Fig.
Optimum protein function and biochemical activity critically depends on water availability because solvent thermodynamics drive protein folding and macromolecular interactions1. 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. Here, within concentrated macromolecular solutions such as the cytosol, we found that modest changes in temperature greatly affect the water potential, and are counteracted by opposing changes in osmotic strength. This duality of temperature and osmotic strength enables simple manipulations of solvent thermodynamics to prevent cell death after extreme cold or heat shock. Physiologically, cells must sustain their activity against fluctuating temperature, pressure and osmotic strength, which impact water availability within seconds. Yet, established mechanisms of water homeostasis act over much slower timescales2,3; we therefore postulated the existence of a rapid compensatory response. We find that this function is performed by water potential-driven changes in macromolecular assembly, particularly biomolecular condensation of intrinsically disordered proteins. The formation and dissolution of biomolecular condensates liberates and captures free water, respectively, quickly counteracting thermal or osmotic perturbations of water potential, which is consequently robustly buffered in the cytoplasm. Our results indicate that biomolecular condensation constitutes an intrinsic biophysical feedback response that rapidly compensates for intracellular osmotic and thermal fluctuations. We suggest that preserving water availability within the concentrated cytosol is an overlooked evolutionary driver of protein (dis)order and function.
Optimum protein function and biochemical activity critically depends on water availability because solvent thermodynamics drive protein folding and macromolecular interactions 1 . 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. Here, within concentrated macromolecular solutions such as the cytosol, we found that modest changes in temperature greatly affect the water potential, and are counteracted by opposing changes in osmotic strength. This duality of temperature and osmotic strength enables simple manipulations of solvent thermodynamics to prevent cell death after extreme cold or heat shock. Physiologically, cells must sustain their activity against fluctuating temperature, pressure and osmotic strength, which impact water availability within seconds. Yet, established mechanisms of water homeostasis act over much slower timescales 2,3 ; we therefore postulated the existence of a rapid compensatory response. We find that this function is performed by water potential-driven changes in macromolecular assembly, particularly biomolecular condensation of intrinsically disordered proteins. The formation and dissolution of biomolecular condensates liberates and captures free water, respectively, quickly counteracting thermal or osmotic perturbations of water potential, which is consequently robustly buffered in the cytoplasm. Our results indicate that biomolecular condensation constitutes an intrinsic biophysical feedback response that rapidly compensates for intracellular osmotic and thermal fluctuations. We suggest that preserving water availability within the concentrated cytosol is an overlooked evolutionary driver of protein (dis)order and function.
Author Derivery, Emmanuel
Krüger, Lara K.
Dudek, Michal
Zeng, Aiwei
Morf, Jörg
O’Neill, John S.
Watson, Joseph L.
Barbiero, Silvia
Vanden Oever, Michael
Stangherlin, Alessandra
Porebski, Benjamin T.
Chambers, Joseph E.
McNally, Kerrie E.
Styles, Christine T.
Mihut, Andrei
Beale, Andrew D.
Wong, David C. S.
Miliotis, Christos
Voorhees, Rebecca M.
Planelles-Herrero, Vicente Jose
Seinkmane, Estere
Brugués, Jan
Edgar, Rachel S.
Riggi, Margot
Guna, Alina
Iwasa, Janet
Rzechorzek, Nina M.
Meng, Qing-Jun
McCall, Patrick M.
Peak-Chew, Sew Yeu
Inglis, Alison J.
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/37853127$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright The Author(s) 2023. corrected publication 2024
2023. The Author(s).
Copyright Nature Publishing Group Nov 23, 2023
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  doi: 10.1091/mbc.01-10-0476
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  publication-title: Phys. Chem. Chem. Phys.
  doi: 10.1039/C6CP08809K
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Snippet Optimum protein function and biochemical activity critically depends on water availability because solvent thermodynamics drive protein folding and...
In other words, water is required to hydrate macromolecules and make them fold properly, but this restricts the movement of water molecules and thereby...
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SubjectTerms 13
13/62
14
14/19
631/45/470
631/57/2269
631/80
631/80/458
Cell Death
Cytosol - chemistry
Cytosol - metabolism
Denaturation
Homeostasis
Humanities and Social Sciences
Hydration
Hydrogen
Intracellular
Kinases
Low temperature
Macromolecular Substances - chemistry
Macromolecular Substances - metabolism
Macromolecules
Molecular dynamics
multidisciplinary
Osmolar Concentration
Pressure
Protein denaturation
Protein folding
Proteins
Proteins - chemistry
Proteins - metabolism
Science
Science (multidisciplinary)
Solvents
Solvents - chemistry
Solvents - metabolism
Temperature
Temperature dependence
Thermodynamics
Time Factors
Water - chemistry
Water - metabolism
Water availability
Water content
Water potential
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Title Macromolecular condensation buffers intracellular water potential
URI https://link.springer.com/article/10.1038/s41586-023-06626-z
https://www.ncbi.nlm.nih.gov/pubmed/37853127
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Volume 623
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