Literature DB >> 22959613

Evolution of the β-barrel assembly machinery.

Chaille T Webb1, Eva Heinz, Trevor Lithgow.   

Abstract

Proteins from the Omp85 family have roles in membrane biogenesis, and the archetypal protein of this family is the bacterial outer membrane protein BamA. Through evolution, BamA has acquired membrane protein partner subunits, but distinct partner subunits are evident in the various bacterial lineages. As a result, experimental work on several species of bacteria has revealed varietal forms of the β-barrel assembly machinery (BAM complex). This scenario extends even into mitochondria and plastids, organelles of eukaryotic cells that evolved from intracellular bacterial ancestors. In addition to the BAM complex, other molecular machines, namely the two-partner secretion system (TPS) and the translocation and assembly module (the TAM), probably evolved from gene duplication events involving BamA. We discuss what is known about the diverse composition of the BAM complex in various bacterial lineages, and how this diversity impacts on our understanding of the mechanism underlying the assembly of bacterial outer membranes.
Copyright © 2012 Elsevier Ltd. All rights reserved.

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Year:  2012        PMID: 22959613     DOI: 10.1016/j.tim.2012.08.006

Source DB:  PubMed          Journal:  Trends Microbiol        ISSN: 0966-842X            Impact factor:   17.079


  56 in total

1.  The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition.

Authors:  Sunyia Hussain; Harris D Bernstein
Journal:  J Biol Chem       Date:  2018-01-08       Impact factor: 5.157

2.  The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping.

Authors:  Begoña Heras; Makrina Totsika; Kate M Peters; Jason J Paxman; Christine L Gee; Russell J Jarrott; Matthew A Perugini; Andrew E Whitten; Mark A Schembri
Journal:  Proc Natl Acad Sci U S A       Date:  2013-12-13       Impact factor: 11.205

Review 3.  The β-barrel assembly machinery in motion.

Authors:  Nicholas Noinaj; James C Gumbart; Susan K Buchanan
Journal:  Nat Rev Microbiol       Date:  2017-02-20       Impact factor: 60.633

4.  Lateral opening and exit pore formation are required for BamA function.

Authors:  Nicholas Noinaj; Adam J Kuszak; Curtis Balusek; James C Gumbart; Susan K Buchanan
Journal:  Structure       Date:  2014-06-26       Impact factor: 5.006

5.  Interfering with outer membrane biogenesis to fight Gram-negative bacterial pathogens.

Authors:  Raffaele Ieva
Journal:  Virulence       Date:  2017-02-17       Impact factor: 5.882

Review 6.  Evolution of protein transport to the chloroplast envelope membranes.

Authors:  Philip M Day; Steven M Theg
Journal:  Photosynth Res       Date:  2018-10-05       Impact factor: 3.573

7.  C-terminal kink formation is required for lateral gating in BamA.

Authors:  Karl Lundquist; Jeremy Bakelar; Nicholas Noinaj; James C Gumbart
Journal:  Proc Natl Acad Sci U S A       Date:  2018-08-07       Impact factor: 11.205

8.  Conformation-specific labeling of BamA and suppressor analysis suggest a cyclic mechanism for β-barrel assembly in Escherichia coli.

Authors:  Nathan W Rigel; Dante P Ricci; Thomas J Silhavy
Journal:  Proc Natl Acad Sci U S A       Date:  2013-03-11       Impact factor: 11.205

9.  Localization of the outer membrane protein OmpA2 in Caulobacter crescentus depends on the position of the gene in the chromosome.

Authors:  Luis David Ginez; Aurora Osorio; Sebastian Poggio
Journal:  J Bacteriol       Date:  2014-06-02       Impact factor: 3.490

10.  Phosphatidylcholine affects the role of the sorting and assembly machinery in the biogenesis of mitochondrial β-barrel proteins.

Authors:  Max-Hinderk Schuler; Francesca Di Bartolomeo; Lena Böttinger; Susanne E Horvath; Lena-Sophie Wenz; Günther Daum; Thomas Becker
Journal:  J Biol Chem       Date:  2015-09-18       Impact factor: 5.157

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