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

    Year: 2014

    Journal: Nature Communications 5, Article number: 5078 doi:10.1038/ncomms6078, 20141029

    Authors: Hsin-Hui Shen, Denisse L. Leyton, Takuya Shiota, Matthew J. Belousoff, Nicholas Noinaj, Jingxiong Lu, Stephen A. Holt, Khershing Tan, Joel Selkrig, Chaille T. Webb, Susan K. Buchanan, Lisandra L. Martin & Trevor Lithgow

    Last authors: Trevor Lithgow

    Organizations: Department of Microbiology, Monash University, Melbourne, Victoria 3800, Australia School of Chemistry, Monash University, Melbourne, Victoria 3800, Australia Department of Chemical Engineering, Monash University, Melbourne, Victoria 3800, Australia NIDDK, NIH, Bethesda, Maryland 20892, USA The Bragg Institute, Australian Nuclear Science and Technology Organization (ANSTO), Lucas Heights, Sydney, New South Wales 2234, Australia

    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.