BAmSA: Visualising transmembrane regions in protein complexes using biotinylated amphipols and electron microscopy.
| dc.rights.license | open | en_US |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | PERRY, Thomas Noe | |
| dc.contributor.author | SOUABNI, Hager | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | RAPISARDA, Chiara | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | FRONZES, Rémi | |
| dc.contributor.author | GIUSTI, Fabrice | |
| dc.contributor.author | POPOT, Jean-Luc | |
| dc.contributor.author | ZOONENS, Manuela | |
| dc.contributor.author | GUBELLINI, Francesca | |
| dc.date.accessioned | 2024-09-30T09:30:41Z | |
| dc.date.available | 2024-09-30T09:30:41Z | |
| dc.date.issued | 2019-02-01 | |
| dc.identifier.issn | 1879-2642 | en_US |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/202014 | |
| dc.description.abstractEn | Membrane protein (MP) complexes play key roles in all living cells. Their structural characterisation is hampered by difficulties in purifying and crystallising them. Recent progress in electron microscopy (EM) have revolutionised the field, not only by providing higher-resolution structures for previously characterised MPs but also by yielding first glimpses into the structure of larger and more challenging complexes, such as bacterial secretion systems. However, the resolution of pioneering EM structures may be difficult and their interpretation requires clues regarding the overall organisation of the complexes. In this context, we present BAmSA, a new method for localising transmembrane (TM) regions in MP complexes, using a general procedure that allows tagging them without resorting to neither genetic nor chemical modification. Labels bound to TM regions can be visualised directly on raw negative-stain EM images, on class averages, or on three-dimensional reconstructions, providing a novel strategy to explore the organisation of MP complexes. | |
| dc.language.iso | EN | en_US |
| dc.subject.en | Animals | |
| dc.subject.en | Biotinylation | |
| dc.subject.en | Cattle | |
| dc.subject.en | Cell Membrane | |
| dc.subject.en | Electron Transport Complex III | |
| dc.subject.en | Escherichia coli Proteins | |
| dc.subject.en | Lipoproteins | |
| dc.subject.en | Membrane Proteins | |
| dc.subject.en | Microscopy | |
| dc.subject.en | Electron | |
| dc.subject.en | Models | |
| dc.subject.en | Molecular | |
| dc.subject.en | Negative Staining | |
| dc.subject.en | Polymers | |
| dc.subject.en | Streptavidin | |
| dc.title.en | BAmSA: Visualising transmembrane regions in protein complexes using biotinylated amphipols and electron microscopy. | |
| dc.title.alternative | Biochim Biophys Acta Biomembr | en_US |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1016/j.bbamem.2018.11.004 | en_US |
| dc.subject.hal | Sciences du Vivant [q-bio]/Microbiologie et Parasitologie | en_US |
| dc.identifier.pubmed | 30444973 | en_US |
| bordeaux.journal | Biochimica et Biophysica Acta:Biomembranes | en_US |
| bordeaux.page | 466-477 | en_US |
| bordeaux.volume | 1861 | en_US |
| bordeaux.hal.laboratories | MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234 | en_US |
| bordeaux.issue | 2 | en_US |
| bordeaux.institution | CNRS | en_US |
| bordeaux.peerReviewed | oui | en_US |
| bordeaux.inpress | non | en_US |
| bordeaux.import.source | pubmed | |
| hal.popular | non | en_US |
| hal.audience | Internationale | en_US |
| hal.export | false | |
| workflow.import.source | pubmed | |
| dc.rights.cc | Pas de Licence CC | en_US |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochimica%20et%20Biophysica%20Acta:Biomembranes&rft.date=2019-02-01&rft.volume=1861&rft.issue=2&rft.spage=466-477&rft.epage=466-477&rft.eissn=1879-2642&rft.issn=1879-2642&rft.au=PERRY,%20Thomas%20Noe&SOUABNI,%20Hager&RAPISARDA,%20Chiara&FRONZES,%20R%C3%A9mi&GIUSTI,%20Fabrice&rft.genre=article |
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