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Please use this identifier to cite or link to this item: http://apo.ansto.gov.au/dspace/handle/10238/7904

Title: Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes
Authors: Shen, H-H
Leyton, DL
Shiota, T
Belousoff, MJ
Noinaj, N
Lu, J
Holt, SA
Tan, K
Selkrig, J
Webb, CT
Buchanan, SK
Martin, LL
Lithgow, T
Keywords: MEMBRANES
PATHOGENS
PROTEINS
MOLECULES
NEUTRON REFLECTORS
PATHOGENS
Issue Date: 24-Oct-2014
Publisher: Macmillan Publishers Limited, part of Springer Nature.
Citation: Shen, H.-H., Leyton, D. L., Shiota, T., Belousoff, M. J., Noinaj, N., Lu, J., . . . Lithgow, T. (2014). Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes. Nature Communications, 5. doi: http://dx.doi.org/10.1038/ncomms6078
Abstract: In 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.
URI: http://dx.doi.org/10.1038/ncomms6078
http://apo.ansto.gov.au/dspace/handle/10238/7904
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