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  • Bilayer-Mediated Clustering and Functional Interaction of MscL Channels

    Author(s)
    Grage, Stephan L
    Keleshian, Asbed M
    Turdzeladze, Tamta
    Battle, Andrew R
    Tay, Wee C
    May, Roland P
    Holt, Stephen A
    Contera, Sonia Antoranz
    Haertlein, Michael
    Moulin, Martine
    Pal, Prithwish
    Rohde, Paul R
    Forsyth, V Trevor
    Watts, Anthony
    Huang, Kerwyn Casey
    Ulrich, Anne S
    Martinac, Boris
    Griffith University Author(s)
    Battle, Andrew
    Year published
    2011
    Metadata
    Show full item record
    Abstract
    Mechanosensitive channels allow bacteria to respond to osmotic stress by opening a nanometer-sized pore in the cellular membrane. Although the underlying mechanism has been thoroughly studied on the basis of individual channels, the behavior of channel ensembles has yet to be elucidated. This work reveals that mechanosensitive channels of large conductance (MscL) exhibit a tendency to spatially cluster, and demonstrates the functional relevance of clustering. We evaluated the spatial distribution of channels in a lipid bilayer using patch-clamp electrophysiology, fluorescence and atomic force microscopy, and neutron scattering ...
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    Mechanosensitive channels allow bacteria to respond to osmotic stress by opening a nanometer-sized pore in the cellular membrane. Although the underlying mechanism has been thoroughly studied on the basis of individual channels, the behavior of channel ensembles has yet to be elucidated. This work reveals that mechanosensitive channels of large conductance (MscL) exhibit a tendency to spatially cluster, and demonstrates the functional relevance of clustering. We evaluated the spatial distribution of channels in a lipid bilayer using patch-clamp electrophysiology, fluorescence and atomic force microscopy, and neutron scattering and reflection techniques, coupled with mathematical modeling of the mechanics of a membrane crowded with proteins. The results indicate that MscL forms clusters under a wide range of conditions. MscL is closely packed within each cluster but is still active and mechanosensitive. However, the channel activity is modulated by the presence of neighboring proteins, indicating membrane-mediated protein-protein interactions. Collectively, these results suggest that MscL self-assembly into channel clusters plays an osmoregulatory functional role in the membrane.
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    Journal Title
    Biophysical Journal
    Volume
    100
    Issue
    5
    DOI
    https://doi.org/10.1016/j.bpj.2011.01.023
    Subject
    Physical sciences
    Biological physics
    Chemical sciences
    Biological sciences
    Publication URI
    http://hdl.handle.net/10072/42845
    Collection
    • Journal articles

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