The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex

The β-barrel assembly machine (BAM) complex is an essential feature of all bacteria with an outer membrane. The core subunit of the BAM complex is BamA and, in Escherichia coli, four lipoprotein subunits: BamB, BamC, BamD and BamE, also function in the BAM complex. Hidden Markov model analysis was u...

Full description

Bibliographic Details
Main Authors:	Anwari, Khatira, Webb, Chaille T, Poggio, Sebastian, Perry, Andrew J, Belousoff, Matthew, Celik, Nermin, Ramm, Georg, Lovering, Andrew, Sockett, R Elizabeth, Smit, John, Jacobs-Wagner, Christine, Lithgow, Trevor
Format:	Online
Language:	English
Published:	Blackwell Publishing Ltd 2012
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3359395/

id	pubmed-3359395
recordtype	oai_dc
spelling	pubmed-33593952013-02-08 The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex Anwari, Khatira Webb, Chaille T Poggio, Sebastian Perry, Andrew J Belousoff, Matthew Celik, Nermin Ramm, Georg Lovering, Andrew Sockett, R Elizabeth Smit, John Jacobs-Wagner, Christine Lithgow, Trevor Research Articles The β-barrel assembly machine (BAM) complex is an essential feature of all bacteria with an outer membrane. The core subunit of the BAM complex is BamA and, in Escherichia coli, four lipoprotein subunits: BamB, BamC, BamD and BamE, also function in the BAM complex. Hidden Markov model analysis was used to comprehensively assess the distribution of subunits of the BAM lipoproteins across all subclasses of proteobacteria. A patchwork distribution was detected which is readily reconciled with the evolution of the α-, β-, γ-, δ- and ε-proteobacteria. Our findings lead to a proposal that the ancestral BAM complex was composed of two subunits: BamA and BamD, and that BamB, BamC and BamE evolved later in a distinct sequence of events. Furthermore, in some lineages novel lipoproteins have evolved instead of the lipoproteins found in E. coli. As an example of this concept, we show that no known species of α-proteobacteria has a homologue of BamC. However, purification of the BAM complex from the model α-proteobacterium Caulobacter crescentus identified a novel subunit we refer to as BamF, which has a conserved sequence motif related to sequences found in BamC. BamF and BamD can be eluted from the BAM complex under similar conditions, mirroring the BamC:D module seen in the BAM complex of γ-proteobacteria such as E. coli. Blackwell Publishing Ltd 2012-06 2012-04-23 /pmc/articles/PMC3359395/ /pubmed/22524202 http://dx.doi.org/10.1111/j.1365-2958.2012.08059.x Text en © 2012 Blackwell Publishing Ltd http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Anwari, Khatira Webb, Chaille T Poggio, Sebastian Perry, Andrew J Belousoff, Matthew Celik, Nermin Ramm, Georg Lovering, Andrew Sockett, R Elizabeth Smit, John Jacobs-Wagner, Christine Lithgow, Trevor
spellingShingle	Anwari, Khatira Webb, Chaille T Poggio, Sebastian Perry, Andrew J Belousoff, Matthew Celik, Nermin Ramm, Georg Lovering, Andrew Sockett, R Elizabeth Smit, John Jacobs-Wagner, Christine Lithgow, Trevor The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex
author_facet	Anwari, Khatira Webb, Chaille T Poggio, Sebastian Perry, Andrew J Belousoff, Matthew Celik, Nermin Ramm, Georg Lovering, Andrew Sockett, R Elizabeth Smit, John Jacobs-Wagner, Christine Lithgow, Trevor
author_sort	Anwari, Khatira
title	The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex
title_short	The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex
title_full	The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex
title_fullStr	The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex
title_full_unstemmed	The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex
title_sort	evolution of new lipoprotein subunits of the bacterial outer membrane bam complex
description	The β-barrel assembly machine (BAM) complex is an essential feature of all bacteria with an outer membrane. The core subunit of the BAM complex is BamA and, in Escherichia coli, four lipoprotein subunits: BamB, BamC, BamD and BamE, also function in the BAM complex. Hidden Markov model analysis was used to comprehensively assess the distribution of subunits of the BAM lipoproteins across all subclasses of proteobacteria. A patchwork distribution was detected which is readily reconciled with the evolution of the α-, β-, γ-, δ- and ε-proteobacteria. Our findings lead to a proposal that the ancestral BAM complex was composed of two subunits: BamA and BamD, and that BamB, BamC and BamE evolved later in a distinct sequence of events. Furthermore, in some lineages novel lipoproteins have evolved instead of the lipoproteins found in E. coli. As an example of this concept, we show that no known species of α-proteobacteria has a homologue of BamC. However, purification of the BAM complex from the model α-proteobacterium Caulobacter crescentus identified a novel subunit we refer to as BamF, which has a conserved sequence motif related to sequences found in BamC. BamF and BamD can be eluted from the BAM complex under similar conditions, mirroring the BamC:D module seen in the BAM complex of γ-proteobacteria such as E. coli.
publisher	Blackwell Publishing Ltd
publishDate	2012
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3359395/
_version_	1611532170660151296

The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex

Similar Items