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Diffusive intracellular interactions: On the role of protein net charge and functional adaptation
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-8204-7798
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0003-0739-2935
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-6048-6896
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2023 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 81, article id 102625Article in journal (Refereed) Published
Abstract [en]

A striking feature of nucleic acids and lipid membranes is that they all carry net negative charge and so is true for the majority of intracellular proteins. It is suggested that the role of this negative charge is to assure a basal intermolecular repulsion that keeps the cytosolic content suitably ‘fluid’ for function. We focus in this review on the experimental, theoretical and genetic findings which serve to underpin this idea and the new questions they raise. Unlike the situation in test tubes, any functional protein-protein interaction in the cytosol is subject to competition from the densely crowded background, i.e. surrounding stickiness. At the nonspecific limit of this stickiness is the ‘random’ protein-protein association, maintaining profuse populations of transient and constantly interconverting complexes at physiological protein concentrations. The phenomenon is readily quantified in studies of the protein rotational diffusion, showing that the more net negatively charged a protein is the less it is retarded by clustering. It is further evident that this dynamic protein-protein interplay is under evolutionary control and finely tuned across organisms to maintain optimal physicochemical conditions for the cellular processes. The emerging picture is then that specific cellular function relies on close competition between numerous weak and strong interactions, and where all parts of the protein surfaces are involved. The outstanding challenge is now to decipher the very basics of this many-body system: how the detailed patterns of charged, polar and hydrophobic side chains not only control protein-protein interactions at close- and long-range but also the collective properties of the cellular interior as a whole.

Place, publisher, year, edition, pages
2023. Vol. 81, article id 102625
National Category
Biophysics
Identifiers
URN: urn:nbn:se:su:diva-219978DOI: 10.1016/j.sbi.2023.102625ISI: 001035521800001PubMedID: 37331204Scopus ID: 2-s2.0-85162160917OAI: oai:DiVA.org:su-219978DiVA, id: diva2:1786858
Available from: 2023-08-10 Created: 2023-08-10 Last updated: 2023-08-30Bibliographically 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)
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Available from: 2023-08-30 Created: 2023-08-10 Last updated: 2023-08-30Bibliographically approved

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Vallina Estrada, EloyZhang, NannanDanielsson, JensOliveberg, Mikael

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