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

Autor:	Selkrig J; 1] Department of Microbiology, Monash University, Clayton 3800, Australia [2] Department of Biochemistry and Molecular Biology, Monash University, Clayton 3800, Australia., Belousoff MJ; Department of Microbiology, Monash University, Clayton 3800, Australia., Headey SJ; Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville 3052, Australia., Heinz E; Department of Microbiology, Monash University, Clayton 3800, Australia., Shiota T; Department of Microbiology, Monash University, Clayton 3800, Australia., Shen HH; 1] Department of Microbiology, Monash University, Clayton 3800, Australia [2] Department of Materials Engineering, Monash University, Clayton 3800, Australia., Beckham SA; Department of Biochemistry and Molecular Biology, Monash University, Clayton 3800, Australia., Bamert RS; Department of Microbiology, Monash University, Clayton 3800, Australia., Phan MD; Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia., Schembri MA; Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia., Wilce MC; Department of Biochemistry and Molecular Biology, Monash University, Clayton 3800, Australia., Scanlon MJ; Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville 3052, Australia., Strugnell RA; Department of Microbiology &Immunology, University of Melbourne, Parkville 3052, Australia., Lithgow T; Department of Microbiology, Monash University, Clayton 3800, Australia.
Jazyk:	angličtina
Zdroj:	Scientific reports [Sci Rep] 2015 Aug 05; Vol. 5, pp. 12905. Date of Electronic Publication: 2015 Aug 05.
DOI:	10.1038/srep12905
Abstrakt:	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.
Databáze:	MEDLINE
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