Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.
Identifieur interne : 001C93 ( PubMed/Corpus ); précédent : 001C92; suivant : 001C94Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.
Auteurs : Alex Dajkovic ; Elizabeth Hinde ; Calum Mackichan ; Rut Carballido-LopezSource :
- PloS one [ 1932-6203 ] ; 2016.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Bacterial Proteins.
- chemical , secretion : Adenosine Triphosphatases, Bacterial Proteins, SEC Translocation Channels.
- metabolism : Bacillus subtilis, Cell Membrane, Cytosol.
- Protein Binding, Protein Transport.
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.
DOI: 10.1371/journal.pone.0157899
PubMed: 27336478
Links to Exploration step
pubmed:27336478Le document en format XML
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<author><name sortKey="Hinde, Elizabeth" sort="Hinde, Elizabeth" uniqKey="Hinde E" first="Elizabeth" last="Hinde">Elizabeth Hinde</name>
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<author><name sortKey="Mackichan, Calum" sort="Mackichan, Calum" uniqKey="Mackichan C" first="Calum" last="Mackichan">Calum Mackichan</name>
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<author><name sortKey="Carballido Lopez, Rut" sort="Carballido Lopez, Rut" uniqKey="Carballido Lopez R" first="Rut" last="Carballido-Lopez">Rut Carballido-Lopez</name>
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<term>Bacterial Proteins (secretion)</term>
<term>Cell Membrane (metabolism)</term>
<term>Cytosol (metabolism)</term>
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<term>SEC Translocation Channels (secretion)</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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