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

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  • Hsin-Hui Shen

    (Monash University, Melbourne, Victoria 3800, Australia
    School of Chemistry, Monash University, Melbourne, Victoria 3800, Australia
    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)

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.

Suggested Citation

  • 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 & Lisan, 2014. "Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6078
    DOI: 10.1038/ncomms6078
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    Cited by:

    1. Xu Wang & Sarah B. Nyenhuis & Harris D. Bernstein, 2024. "The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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