Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry
Open accessAbstract
Innovating to be nondisruptive: Insights into the architecture and stoichiometry of membrane complexes have grown with advances in cryo–electron microscopy and native mass spectroscopy. However, most of these studies are not in the context of native membrane. Chorev et al. released intact membrane complexes directly from native lipid membrane vesicles into a mass spectrometer. They analyzed components of the Escherichia coli inner and outer membranes and the bovine mitochondrial inner membrane. For several identified complexes, they found a stoichiometry that differs from published results and, in some cases, confirmed interactions that could not be characterized structurally. Science , this issue p. 829
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Robinson and coworkers demonstrated native MS analysis of protein assemblies directly from native membranes without detergents.
“Robinson and coworkers have successfully demonstrated native MS analysis for a number of applications including most recently analyzing protein assemblies directly for native membranes bypassing the use of detergents [51].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [51]
Many challenging analytes such as membrane proteins, intrinsically disordered proteins, highly dynamic or heterogeneous complexes, or very large systems such as intact virus capsids can all be investigated using native MS, as well as their associated proteoforms.
“By using appropriate sample preparation, ionisation conditions, and instrumentation, many challenging analytes such as membrane proteins,18,42 intrinsically disordered proteins,43 highly dynamic or heterogeneous complexes,19 or very large systems such as intact virus capsids44 can all be investigated using native MS, as well as their associated proteoforms.45”
From Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry (2020) · cites this paper as [42]
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- Authors
- Chorev, D. S., Baker, L. A., Wu, D., Beilsten-Edmands, V., Rouse, S. L., Zeev-Ben-Mordehai, T., Jiko, C., Samsudin, F., Gerle, C., Khalid, S., Stewart, A. G., Matthews, S. J., Grünewald, K., & Robinson, C. V.
- Affiliations
- University of Oxford (GB)
- Imperial College London (GB)
- Division of Structural Biology, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
- Institute for Integrated Radiation and Nuclear Science, Kyoto University (JP)
- University of Southampton (GB)
- Japan Science and Technology Agency (JP)
- Victor Chang Cardiac Research Institute (AU)
- Universität Hamburg (DE)
- Corresponding author
- Robinson, Carol V.
- ORCID
- Venue
- Science
- Published
- 2018-11-16
- Volume
- 362
- Issue
- 6416
- Pages
- 829-834
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC6522346
- OpenAlex
- W2901712030
- Cited by
- 191
- References
- 63
- Citations by year
- 2026: 11 · 2025: 16 · 2024: 19 · 2023: 26 · 2022: 24 · 2021: 28 · 2020: 33 · 2019: 32 · 2018: 2
- FWCI
- 10.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Funders
- Wellcome Trust (104633/Z/14/Z, 090895/Z/09/Z)
- BBSRC (BB/M029573/1)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- membrane protein complexes, Escherichia coli inner membrane, Escherichia coli outer membrane, protein-protein interaction, native mass spectrometry
- MeSH terms
- SEC Translocation Channels, Protein Conformation, beta-Strand, Animals, Bacterial Outer Membrane Proteins, Bacterial Proteins, Cattle, Lipid Bilayers, Membrane Proteins, Mass Spectrometry, Porins, Molecular Chaperones, Proteome, Mitochondrial Proton-Translocating ATPases, Escherichia coli Proteins, Adenine Nucleotide Translocator 1, Mitochondrial Membranes
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