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Colloidal stability of the living cell
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-6048-6896
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 42020 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 117, no 19, p. 10113-10121Article in journal (Refereed) Published
Abstract [en]

Cellular function is generally depicted at the level of functional pathways and detailed structural mechanisms, based on the identification of specific protein-protein interactions. For an individual protein searching for its partner, however, the perspective is quite different: The functional task is challenged by a dense crowd of nonpartners obstructing the way. Adding to the challenge, there is little information about how to navigate the search, since the encountered surrounding is composed of protein surfaces that are predominantly nonconserved or, at least, highly variable across organisms. In this study, we demonstrate from a colloidal standpoint that such a blindfolded intracellular search is indeed favored and has more fundamental impact on the cellular organization than previously anticipated. Basically, the unique polyion composition of cellular systems renders the electrostatic interactions different from those in physiological buffer, leading to a situation where the protein net-charge density balances the attractive dispersion force and surface heterogeneity at close range. Inspection of naturally occurring proteomes and in-cell NMR data show further that the nonconserved protein surfaces are by no means passive but chemically biased to varying degree of net-negative repulsion across organisms. Finally, this electrostatic control explains how protein crowding is spontaneously maintained at a constant level through the intracellular osmotic pressure and leads to the prediction that the extreme in halophilic adaptation is not the ionic-liquid conditions per se but the evolutionary barrier of crossing its physicochemical boundaries.

Place, publisher, year, edition, pages
2020. Vol. 117, no 19, p. 10113-10121
Keywords [en]
cellular organization, protein-protein interactions, electrostatics, halophilic adaptation, ion screening
National Category
Biological Sciences Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-183002DOI: 10.1073/pnas.1914599117ISI: 000532837500005PubMedID: 32284426OAI: oai:DiVA.org:su-183002DiVA, id: diva2:1450659
Available from: 2020-07-01 Created: 2020-07-01 Last updated: 2023-08-10Bibliographically approved
In thesis
1. Navigating the Cellular Crowd: Physicochemical Properties of Protein Surfaces as Evolved Interaction Guides
Open this publication in new window or tab >>Navigating the Cellular Crowd: Physicochemical Properties of Protein Surfaces as Evolved Interaction Guides
2023 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The cellular interior is characterised by high concentrations of macromolecules. Compared with dilute conditions, the crowd modifies proteins' ability to fold, diffuse and, ultimately, carry out their biological functions. Cellular fitness depends on ensuring an adequate balance between interactivity and diffusivity.

In this thesis, I discuss how a colloidal description of the cell highlights the central role of electrostatics in protein surface optimisation. By recognising that the modulation of protein-protein interactions concerns the whole proteome, I map the physicochemical preferences of cellular organisms across taxonomic and ecological divisions. Moreover, I propose that all surface residues participate in tuning protein interactions to the correct affinity, within a continuum that spans several orders of magnitude. Finally, I turn to horizontally spreading inteins to gauge the strength of the selective pressures acting on protein surfaces.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2023. p. 47
Keywords
protein interactions, inteins, physicochemical properties, protein surfaces, evolution, cellular crowding, electrostatics
National Category
Biophysics
Research subject
Biophysics
Identifiers
urn:nbn:se:su:diva-219982 (URN)978-91-8014-408-7 (ISBN)978-91-8014-409-4 (ISBN)
Public defence
2023-09-22, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16B, Stockholm, 09:00 (English)
Opponent
Supervisors
Available from: 2023-08-30 Created: 2023-08-10 Last updated: 2023-08-30Bibliographically approved

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Estrada, Eloy VallinaDanielsson, JensOliveberg, Mikael

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