PERRY, Thomas Noe; SOUABNI, Hager; RAPISARDA, Chiara; FRONZES, Rémi; GIUSTI, Fabrice; POPOT, Jean-Luc; ZOONENS, Manuela; GUBELLINI, Francesca

doi:10.1016/j.bbamem.2018.11.004

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PERRY, Thomas Noe
Microbiologie Fondamentale et Pathogénicité [MFP]

SOUABNI, Hager

RAPISARDA, Chiara
Microbiologie Fondamentale et Pathogénicité [MFP]

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Biochimica et Biophysica Acta:Biomembranes. 2019-02-01, vol. 1861, n° 2, p. 466-477

Résumé en anglais

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.< Réduire

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Animals

Biotinylation

Cattle

Cell Membrane

Electron Transport Complex III

Escherichia coli Proteins

Lipoproteins

Membrane Proteins

Microscopy

Electron

Models

Molecular

Negative Staining

Polymers

Streptavidin

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BAmSA: Visualising transmembrane regions in protein complexes using biotinylated amphipols and electron microscopy.

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