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Physicochemical code for quinary protein interactions in Escherichia coli
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 7
2017 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 114, no 23, E4556-E4563 p.Article in journal (Refereed) Published
Abstract [en]

How proteins sense and navigate the cellular interior to find their functional partners remains poorly understood. An intriguing aspect of this search is that it relies on diffusive encounters with the crowded cellular background, made up of protein surfaces that are largely nonconserved. The question is then if/how this protein search is amenable to selection and biological control. To shed light on this issue, we examined the motions of three evolutionary divergent proteins in the Escherichia coli cytoplasm by in-cell NMR. The results show that the diffusive in-cell motions, after all, follow simplistic physical-chemical rules: The proteins reveal a common dependence on (i) net charge density, (ii) surface hydrophobicity, and (iii) the electric dipole moment. The bacterial protein is here biased to move relatively freely in the bacterial interior, whereas the human counterparts more easily stick. Even so, the in-cell motions respond predictably to surface mutation, allowing us to tune and intermix the protein's behavior at will. The findings show how evolution can swiftly optimize the diffuse background of protein encounter complexes by just single-point mutations, and provide a rational framework for adjusting the cytoplasmic motions of individual proteins, e.g., for rescuing poor in-cell NMR signals and for optimizing protein therapeutics.

Place, publisher, year, edition, pages
2017. Vol. 114, no 23, E4556-E4563 p.
Keyword [en]
in-cell NMR, protein surface properties, intracellular diffusion
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-144791DOI: 10.1073/pnas.1621227114ISI: 000402703800006PubMedID: 28536196OAI: oai:DiVA.org:su-144791DiVA: diva2:1123283
Available from: 2017-07-13 Created: 2017-07-13 Last updated: 2017-07-13Bibliographically approved

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Mu, XinChoi, SeongilLang, LisaDanielsson, JensOliveberg, Mikael
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