title: Global structural changes of an ion channel during its gating are followed by ion mobility mass spectrometry.
abstract: Mechanosensitive ion channels are sensors probing membrane tension in all species; despite their importance and vital role in many cell functions, their gating mechanism remains to be elucidated. Here, we determined the conditions for releasing intact mechanosensitive channel of large conductance (MscL) proteins from their detergents in the gas phase using native ion mobility-mass spectrometry (IM-MS). By using IM-MS, we could detect the native mass of MscL from Escherichia coli, determine various global structural changes during its gating by measuring the rotationally averaged collision cross-sections, and show that it can function in the absence of a lipid bilayer. We could detect global conformational changes during MscL gating as small as 3%. Our findings will allow studying native structure of many other membrane proteins.
authors.affiliation: Biomolecular & Analytical Mass Spectrometry Group and.
authors.forename: Albert
authors.initials: A
authors.lastname: Konijnenberg
authors.affiliation: Department of Biochemistry and.
authors.forename: Duygu
authors.initials: D
authors.lastname: Yilmaz
authors.affiliation: Department of Biochemistry and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG, Groningen, The Netherlands;
authors.forename: Helgi I
authors.initials: HI
authors.lastname: Ingólfsson
authors.affiliation: Department of Biochemistry and.
authors.forename: Anna
authors.initials: A
authors.lastname: Dimitrova
authors.affiliation: Department of Biochemistry and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG, Groningen, The Netherlands;
authors.forename: Siewert J
authors.initials: SJ
authors.lastname: Marrink
authors.affiliation: Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie, Sorbonne Universités, CNRS UMR 7590, Université Pierre et Marie Curie, 75005 Paris, France; and.
authors.forename: Zhuolun
authors.initials: Z
authors.lastname: Li
authors.affiliation: Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie, Sorbonne Universités, CNRS UMR 7590, Université Pierre et Marie Curie, 75005 Paris, France; and.
authors.forename: Catherine
authors.initials: C
authors.lastname: Vénien-Bryan
authors.affiliation: Biomolecular & Analytical Mass Spectrometry Group and UA-VITO Center for Proteomics (CFP-CEPROMA), University of Antwerp, 2020 Antwerp, Belgium; a.kocer@umcg.nl frank.sobott@uantwerpen.be.
authors.forename: Frank
authors.initials: F
authors.lastname: Sobott
authors.affiliation: Department of Neuroscience, University of Groningen, University Medical Center Groningen, 9713 AV, Groningen, The Netherlands a.kocer@umcg.nl frank.sobott@uantwerpen.be.
authors.forename: Armağan
authors.initials: A
authors.lastname: Koçer
mesh_terms: D003902:Detergents / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure; D015640:Ion Channel Gating / Q000502:physiology*; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D013058:Mass Spectrometry / Q000379:methods*; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure; D008854:Microscopy, Electron; D056004:Molecular Dynamics Simulation; D017830:Octoxynol / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D003902:Detergents; D029968:Escherichia coli Proteins; D007473:Ion Channels; D008565:Membrane Proteins; C086596:MscL protein, E coli; D017830:Octoxynol
keywords: MscL; ion channel gating; ion mobility mass spectrometry; membrane proteins; structure function