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

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 and Trevor Lithgow ()
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Hsin-Hui Shen: Monash University, Melbourne, Victoria 3800, Australia
Denisse L. Leyton: Monash University, Melbourne, Victoria 3800, Australia
Takuya Shiota: Monash University, Melbourne, Victoria 3800, Australia
Matthew J. Belousoff: Monash University, Melbourne, Victoria 3800, Australia
Nicholas Noinaj: NIDDK, NIH, Bethesda, Maryland 20892, USA
Jingxiong Lu: Monash University, Melbourne, Victoria 3800, Australia
Stephen A. Holt: The Bragg Institute, Australian Nuclear Science and Technology Organization (ANSTO), Lucas Heights, Sydney, New South Wales 2234, Australia
Khershing Tan: Monash University, Melbourne, Victoria 3800, Australia
Joel Selkrig: Monash University, Melbourne, Victoria 3800, Australia
Chaille T. Webb: Monash University, Melbourne, Victoria 3800, Australia
Susan K. Buchanan: NIDDK, NIH, Bethesda, Maryland 20892, USA
Lisandra L. Martin: School of Chemistry, Monash University, Melbourne, Victoria 3800, Australia
Trevor Lithgow: Monash University, Melbourne, Victoria 3800, Australia

Nature Communications, 2014, vol. 5, issue 1, 1-10

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6078

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