Show simple item record

dc.contributor.authorDajkovic, A
dc.contributor.authorHinde, E
dc.contributor.authorMacKichan, C
dc.contributor.authorCarballido-Lopez, R
dc.date.accessioned2020-12-17T03:54:55Z
dc.date.available2020-12-17T03:54:55Z
dc.date.issued2016
dc.identifierpii: PONE-D-16-11388
dc.identifier.citationDajkovic, 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.
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/11343/255086
dc.description.abstractIn 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.
dc.languageeng
dc.publisherPublic Library of Science (PLoS)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleDynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.
dc.typeJournal Article
dc.identifier.doi10.1371/journal.pone.0157899
melbourne.affiliation.departmentSchool of Physics
melbourne.source.titlePLoS One
melbourne.source.volume11
melbourne.source.issue6
melbourne.source.pagese0157899-
dc.rights.licenseCC BY
melbourne.elementsid1234117
melbourne.openaccess.pmchttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4918944
melbourne.contributor.authorHinde, Elizabeth
dc.identifier.eissn1932-6203
melbourne.accessrightsOpen Access


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record