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    Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.

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    Author
    Dajkovic, A; Hinde, E; MacKichan, C; Carballido-Lopez, R
    Date
    2016
    Source Title
    PLoS One
    Publisher
    Public Library of Science (PLoS)
    University of Melbourne Author/s
    Hinde, Elizabeth
    Affiliation
    School of Physics
    Metadata
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    Document Type
    Journal Article
    Citations
    Dajkovic, A., Hinde, E., MacKichan, C. & Carballido-Lopez, R. (2016). Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.. PLoS One, 11 (6), pp.e0157899-. https://doi.org/10.1371/journal.pone.0157899.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/255086
    DOI
    10.1371/journal.pone.0157899
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4918944
    Abstract
    In prokaryotes, about one third of cellular proteins are translocated across the plasma membrane or inserted into it by concerted action of the cytoplasmic ATPase SecA and the universally conserved SecYEG heterotrimeric polypeptide-translocating pore. Secretion complexes have been reported to localize in specific subcellular sites in Bacillus subtilis. In this work, we used a combination of total internal reflection microscopy, scanning fluorescence correlation spectroscopy, and pair correlation function to study the localization and dynamics of SecA and SecY in growing Bacillus subtilis cells. Both SecA and SecY localized in transient and dynamic foci in the cytoplasmic membrane, which displayed no higher-level organization in helices. Foci of SecA and SecY were in constant flux with freely diffusing SecA and SecY molecules. Scanning FCS confirmed the existence of populations of cellular SecA and SecY molecules with a wide range of diffusion coefficients. Diffusion of SecY as an uncomplexed molecular species was short-lived and only local while SecY complexed with its protein partners traversed distances of over half a micrometer in the cell.

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