Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes

Simple item page
dc.contributor.authorShen, HHen_AU
dc.contributor.authorLeyton, DLen_AU
dc.contributor.authorShiota, Ten_AU
dc.contributor.authorBelousoff, MJen_AU
dc.contributor.authorNoinaj, Nen_AU
dc.contributor.authorLu, Jen_AU
dc.contributor.authorHolt, SAen_AU
dc.contributor.authorTan, Ken_AU
dc.contributor.authorSelkrig, Jen_AU
dc.contributor.authorWebb, CTen_AU
dc.contributor.authorBuchanan, SKen_AU
dc.contributor.authorMartin, LLen_AU
dc.contributor.authorLithgow, Ten_AU
dc.date.accessioned2016-10-26T00:52:49Zen_AU
dc.date.available2016-10-26T00:52:49Zen_AU
dc.date.issued2014-10-24en_AU
dc.date.statistics2016-10-26en_AU
dc.description.abstractIn biological membranes, various protein secretion devices function as nanomachines, and measuring the internal movements of their component parts is a major technological challenge. The translocation and assembly module (TAM) is a nanomachine required for virulence of bacterial pathogens. We have reconstituted a membrane containing the TAM onto a gold surface for characterization by quartz crystal microbalance with dissipation (QCM-D) and magnetic contrast neutron reflectrometry (MCNR). The MCNR studies provided structural resolution down to 1 Å, enabling accurate measurement of protein domains projecting from the membrane layer. Here we show that dynamic movements within the TamA component of the TAM are initiated in the presence of a substrate protein, Ag43, and that these movements recapitulate an initial stage in membrane protein assembly. The reconstituted system provides a powerful new means to study molecular movements in biological membranes, and the technology is widely applicable to studying the dynamics of diverse cellular nanomachines. © Macmillan Publishers Limiteden_AU
dc.identifier.articlenumber5078en_AU
dc.identifier.citationShen, H.-H., Leyton, D. L., Shiota, T., Belousoff, M. J., Noinaj, N., Lu, J., Holt, S. A., Tan, K., Selkrig, J., Webb, C. T., Buchanan, S. K., Martin, L. L., & Lithgow, T. (2014). Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes. Nature Communications, 5, 1-10, 5078. doi:10.1038/ncomms6078en_AU
dc.identifier.govdoc7439en_AU
dc.identifier.issn2041-1723en_AU
dc.identifier.journaltitleNature Communicationsen_AU
dc.identifier.pagination1-10en_AU
dc.identifier.urihttp://dx.doi.org/10.1038/ncomms6078en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/7904en_AU
dc.identifier.volume5en_AU
dc.language.isoenen_AU
dc.publisherMacmillan Publishers Limited.en_AU
dc.subjectMembranesen_AU
dc.subjectPathogensen_AU
dc.subjectProteinsen_AU
dc.subjectMoleculesen_AU
dc.subjectNeutron reflectorsen_AU
dc.subjectPathogensen_AU
dc.titleReconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranesen_AU
dc.typeJournal Articleen_AU
Files
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.71 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Journal Articles