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

The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex.
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DOI:
10.1111/j.1365-2958.2012.08059.x
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发表时间:
2012-06
影响因子:
3.6
通讯作者:
Lithgow T
Lithgow T
中科院分区:
生物学2区
文献类型:
--
作者:
Anwari K;Webb CT;Poggio S;Perry AJ;Belousoff M;Celik N;Ramm G;Lovering A;Sockett RE;Smit J;Jacobs-Wagner C;Lithgow T

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β-桶组装机(BAM)复合体是所有具有外膜的细菌的基本特征。BAM复合体的核心亚基是BamA,在大肠杆菌中,四个脂蛋白亚基:BamB、BamC、BamD和BamE也在BAM复合体中起作用。隐马尔可夫模型分析用于综合评估BAM脂蛋白亚基在所有变形菌亚类中的分布。发现了一个拼凑分布,这很容易与α-, β-, γ-, δ-和ε-变形菌的进化相一致。我们的研究结果提出,祖先的BAM复合体由两个亚基组成:BamA和BamD, BamB、BamC和BamE后来在一个不同的事件序列中进化。此外,在一些谱系中,进化出了新的脂蛋白,而不是大肠杆菌中的脂蛋白。作为这一概念的一个例子,我们发现没有已知的α-变形菌属物种具有BamC的同源物。然而,从模型α-弯茎杆菌中纯化出BAM复合体,发现了一个新的亚基BamF,该亚基具有与BamC中发现的序列相关的保守序列基序。BamF和BamD可以在相似的条件下从BAM复合物中洗脱出来,这反映了在大肠杆菌等γ-变形菌的BAM复合物中看到的BamC:D模块。
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.
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