Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module.

Selkrig, Joel, Belousoff, Matthew J., Headey, Stephen J., Heinz, Eva, Shiota, Takuya, Shen, Hsin-Hui, Beckham, Simone A., Bamert, Rebecca S., Phan, Minh-Duy, Schembri, Mark A., Wilce, Matthew C.J., Scanlon, Martin J., Strugnell, Richard A. and Lithgow, Trevor (2015) Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module.. Scientific Reports, 5 . doi:10.1038/srep12905


Author Selkrig, Joel
Belousoff, Matthew J.
Headey, Stephen J.
Heinz, Eva
Shiota, Takuya
Shen, Hsin-Hui
Beckham, Simone A.
Bamert, Rebecca S.
Phan, Minh-Duy
Schembri, Mark A.
Wilce, Matthew C.J.
Scanlon, Martin J.
Strugnell, Richard A.
Lithgow, Trevor
Title Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module.
Journal name Scientific Reports   Check publisher's open access policy
ISSN 2045-2322
Publication date 2015-08-05
Sub-type Article (original research)
DOI 10.1038/srep12905
Open Access Status DOI
Volume 5
Total pages 12
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Collection year 2016
Language eng
Formatted abstract
The biogenesis of membranes from constituent proteins and lipids is a fundamental aspect of cell biology. In the case of proteins assembled into bacterial outer membranes, an overarching question concerns how the energy required for protein insertion and folding is accessed at this remote location of the cell. The translocation and assembly module (TAM) is a nanomachine that functions in outer membrane biogenesis and virulence in diverse bacterial pathogens. Here we demonstrate the interactions through which TamA and TamB subunits dock to bridge the periplasm, and unite the outer membrane aspects to the inner membrane of the bacterial cell. We show that specific functional features in TamA have been conserved through evolution, including residues surrounding the lateral gate and an extensive surface of the POTRA domains. Analysis by nuclear magnetic resonance spectroscopy and small angle X-ray scattering document the characteristic structural features of these POTRA domains and demonstrate rigidity in solution. Quartz crystal microbalance measurements pinpoint which POTRA domain specifically docks the TamB subunit of the nanomachine. We speculate that the POTRA domain of TamA functions as a lever arm in order to drive the activity of the TAM, assembling proteins into bacterial outer membranes.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article # 12905

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Mon, 17 Aug 2015, 15:55:49 EST by Prycilla Rehm on behalf of School of Chemistry & Molecular Biosciences