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A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus
Mitochondria are organelles derived from an intracellular α-proteobacterium. The biogenesis of mitochondria relies on the assembly of β-barrel proteins into the mitochondrial outer membrane, a process inherited from the bacterial ancestor. Caulobacter crescentus is an α-proteobacterium, and the BAM...
Autores principales: | , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797634/ https://www.ncbi.nlm.nih.gov/pubmed/20062535 http://dx.doi.org/10.1371/journal.pone.0008619 |
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author | Anwari, Khatira Poggio, Sebastian Perry, Andrew Gatsos, Xenia Ramarathinam, Sri Harsha Williamson, Nicholas A. Noinaj, Nicholas Buchanan, Susan Gabriel, Kipros Purcell, Anthony W. Jacobs-Wagner, Christine Lithgow, Trevor |
author_facet | Anwari, Khatira Poggio, Sebastian Perry, Andrew Gatsos, Xenia Ramarathinam, Sri Harsha Williamson, Nicholas A. Noinaj, Nicholas Buchanan, Susan Gabriel, Kipros Purcell, Anthony W. Jacobs-Wagner, Christine Lithgow, Trevor |
author_sort | Anwari, Khatira |
collection | PubMed |
description | Mitochondria are organelles derived from an intracellular α-proteobacterium. The biogenesis of mitochondria relies on the assembly of β-barrel proteins into the mitochondrial outer membrane, a process inherited from the bacterial ancestor. Caulobacter crescentus is an α-proteobacterium, and the BAM (β-barrel assembly machinery) complex was purified and characterized from this model organism. Like the mitochondrial sorting and assembly machinery complex, we find the BAM complex to be modular in nature. A ∼150 kDa core BAM complex containing BamA, BamB, BamD, and BamE associates with additional modules in the outer membrane. One of these modules, Pal, is a lipoprotein that provides a means for anchorage to the peptidoglycan layer of the cell wall. We suggest the modular design of the BAM complex facilitates access to substrates from the protein translocase in the inner membrane. |
format | Text |
id | pubmed-2797634 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-27976342010-01-09 A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus Anwari, Khatira Poggio, Sebastian Perry, Andrew Gatsos, Xenia Ramarathinam, Sri Harsha Williamson, Nicholas A. Noinaj, Nicholas Buchanan, Susan Gabriel, Kipros Purcell, Anthony W. Jacobs-Wagner, Christine Lithgow, Trevor PLoS One Research Article Mitochondria are organelles derived from an intracellular α-proteobacterium. The biogenesis of mitochondria relies on the assembly of β-barrel proteins into the mitochondrial outer membrane, a process inherited from the bacterial ancestor. Caulobacter crescentus is an α-proteobacterium, and the BAM (β-barrel assembly machinery) complex was purified and characterized from this model organism. Like the mitochondrial sorting and assembly machinery complex, we find the BAM complex to be modular in nature. A ∼150 kDa core BAM complex containing BamA, BamB, BamD, and BamE associates with additional modules in the outer membrane. One of these modules, Pal, is a lipoprotein that provides a means for anchorage to the peptidoglycan layer of the cell wall. We suggest the modular design of the BAM complex facilitates access to substrates from the protein translocase in the inner membrane. Public Library of Science 2010-01-08 /pmc/articles/PMC2797634/ /pubmed/20062535 http://dx.doi.org/10.1371/journal.pone.0008619 Text en This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. |
spellingShingle | Research Article Anwari, Khatira Poggio, Sebastian Perry, Andrew Gatsos, Xenia Ramarathinam, Sri Harsha Williamson, Nicholas A. Noinaj, Nicholas Buchanan, Susan Gabriel, Kipros Purcell, Anthony W. Jacobs-Wagner, Christine Lithgow, Trevor A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus |
title | A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus
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title_full | A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus
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title_fullStr | A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus
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title_full_unstemmed | A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus
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title_short | A Modular BAM Complex in the Outer Membrane of the α-Proteobacterium Caulobacter crescentus
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title_sort | modular bam complex in the outer membrane of the α-proteobacterium caulobacter crescentus |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797634/ https://www.ncbi.nlm.nih.gov/pubmed/20062535 http://dx.doi.org/10.1371/journal.pone.0008619 |
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