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Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module
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 o...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4525385/ https://www.ncbi.nlm.nih.gov/pubmed/26243377 http://dx.doi.org/10.1038/srep12905 |
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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 |
author_facet | 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 |
author_sort | Selkrig, Joel |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4525385 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-45253852015-08-06 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. Lithgow, Trevor Sci Rep Article 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. Nature Publishing Group 2015-08-05 /pmc/articles/PMC4525385/ /pubmed/26243377 http://dx.doi.org/10.1038/srep12905 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article 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 Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module |
title | Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module |
title_full | Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module |
title_fullStr | Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module |
title_full_unstemmed | Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module |
title_short | Conserved features in TamA enable interaction with TamB to drive the activity of the translocation and assembly module |
title_sort | conserved features in tama enable interaction with tamb to drive the activity of the translocation and assembly module |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4525385/ https://www.ncbi.nlm.nih.gov/pubmed/26243377 http://dx.doi.org/10.1038/srep12905 |
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