The role of hydrophobic matching on transmembrane helix packing in cells

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dc.contributor University of Helsinki, Department of Physics en
dc.contributor University of Helsinki, Department of Physics en
dc.contributor University of Helsinki, Department of Physics en
dc.contributor.author Grau, Brayan
dc.contributor.author Javanainen, Matti
dc.contributor.author Jesús García-Murria, Maria
dc.contributor.author Kulig, Waldemar
dc.contributor.author Vattulainen, Ilpo Tapio
dc.contributor.author Mingarro, Ismael
dc.contributor.author Martinez-Gil, Luis
dc.date.accessioned 2018-01-19T13:51:00Z
dc.date.available 2018-01-19T13:51:00Z
dc.date.issued 2017
dc.identifier.citation Grau , B , Javanainen , M , Jesús García-Murria , M , Kulig , W , Vattulainen , I T , Mingarro , I & Martinez-Gil , L 2017 , ' The role of hydrophobic matching on transmembrane helix packing in cells ' , Cell Stress , vol. 1 , no. 2 , pp. 90-106 . https://doi.org/10.15698/cst2017.11.111 en
dc.identifier.issn 2523-0204
dc.identifier.other PURE: 95244252
dc.identifier.other PURE UUID: 147c2672-b68d-41d5-be6a-a0788499150d
dc.identifier.other ORCID: /0000-0001-7568-0029/work/40902824
dc.identifier.other ORCID: /0000-0001-7408-3214/work/40901437
dc.identifier.other ORCID: /0000-0003-4858-364X/work/40903054
dc.identifier.other WOS: 000588293100003
dc.identifier.uri http://hdl.handle.net/10138/231331
dc.description.abstract Folding and packing of membrane proteins are highly influenced by the lipidic component of the membrane. Here, we explore how the hydrophobic mismatch (the difference between the hydrophobic span of a transmembrane protein region and the hydrophobic thickness of the lipid membrane around the protein) influences transmembrane helix packing in a cellular environment. Using a ToxRED assay in Escherichia coli and a Bimolecular Fluorescent Complementation approach in human-derived cells complemented by atomistic molecular dynamics simulations we analyzed the dimerization of Glycophorin A derived transmembrane segments. We concluded that, biological membranes can accommodate transmembrane homo-dimers with a wide range of hydrophobic lengths. Hydrophobic mismatch and its effects on dimerization are found to be considerably weaker than those previously observed in model membranes, or under in vitro conditions, indicating that biological membranes (particularly eukaryotic membranes) can adapt to structural deformations through compensatory mechanisms that emerge from their complex structure and composition to alleviate membrane stress. Results based on atomistic simulations support this view, as they revealed that Glycophorin A dimers remain stable, despite of poor hydrophobic match, using mechanisms based on dimer tilting or local membrane thickness perturbations. Furthermore, hetero-dimers with large length disparity between their monomers are also tolerated in cells, and the conclusions that one can draw are essentially similar to those found with homo-dimers. However, large differences between transmembrane helices length hinder the monomer/dimer equilibrium, confirming that, the hydrophobic mismatch has, nonetheless, biologically relevant effects on helix packing in vivo. en
dc.format.extent 17
dc.language.iso eng
dc.relation.ispartof Cell Stress
dc.rights en
dc.subject 114 Physical sciences en
dc.title The role of hydrophobic matching on transmembrane helix packing in cells en
dc.type Article
dc.description.version Peer reviewed
dc.identifier.doi https://doi.org/10.15698/cst2017.11.111
dc.type.uri info:eu-repo/semantics/other
dc.type.uri info:eu-repo/semantics/publishedVersion
dc.contributor.pbl

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