Literature DB >> 21893027

The Bam machine: a molecular cooper.

Dante P Ricci1, Thomas J Silhavy.   

Abstract

The bacterial outer membrane (OM) is an exceptional biological structure with a unique composition that contributes significantly to the resiliency of Gram-negative bacteria. Since all OM components are synthesized in the cytosol, the cell must efficiently transport OM-specific lipids and proteins across the cell envelope and stably integrate them into a growing membrane. In this review, we discuss the challenges associated with these processes and detail the elegant solutions that cells have evolved to address the topological problem of OM biogenesis. Special attention will be paid to the Bam machine, a highly conserved multiprotein complex that facilitates OM β-barrel folding. This article is part of a Special Issue entitled: Protein Folding in Membranes. Copyright Â
© 2011 Elsevier B.V. All rights reserved.

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Year:  2011        PMID: 21893027      PMCID: PMC3253334          DOI: 10.1016/j.bbamem.2011.08.020

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  201 in total

1.  Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.

Authors:  Paula V Bulieris; Susanne Behrens; Otto Holst; Jörg H Kleinschmidt
Journal:  J Biol Chem       Date:  2002-12-30       Impact factor: 5.157

2.  POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins.

Authors:  Luis Sánchez-Pulido; Damien Devos; Stéphanie Genevrois; Miguel Vicente; Alfonso Valencia
Journal:  Trends Biochem Sci       Date:  2003-10       Impact factor: 13.807

3.  Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli.

Authors:  Tao Wu; Andrew C McCandlish; Luisa S Gronenberg; Shu-Sin Chng; Thomas J Silhavy; Daniel Kahne
Journal:  Proc Natl Acad Sci U S A       Date:  2006-07-21       Impact factor: 11.205

4.  Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin.

Authors:  Ingrid Guilvout; Mohamed Chami; Andreas Engel; Anthony P Pugsley; Nicolas Bayan
Journal:  EMBO J       Date:  2006-11-02       Impact factor: 11.598

5.  Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands.

Authors:  Angela A Lilly; Jennine M Crane; Linda L Randall
Journal:  Protein Sci       Date:  2009-09       Impact factor: 6.725

6.  Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface.

Authors:  Martine P Bos; Boris Tefsen; Jeroen Geurtsen; Jan Tommassen
Journal:  Proc Natl Acad Sci U S A       Date:  2004-06-10       Impact factor: 11.205

7.  Novel structure of the conserved gram-negative lipopolysaccharide transport protein A and mutagenesis analysis.

Authors:  Michael D L Suits; Paola Sperandeo; Gianni Dehò; Alessandra Polissi; Zongchao Jia
Journal:  J Mol Biol       Date:  2008-04-26       Impact factor: 5.469

8.  Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics.

Authors:  Didier Vertommen; Natividad Ruiz; Pauline Leverrier; Thomas J Silhavy; Jean-François Collet
Journal:  Proteomics       Date:  2009-05       Impact factor: 3.984

9.  Complete reconstitution of an ATP-binding cassette transporter LolCDE complex from separately isolated subunits.

Authors:  Kyoko Kanamaru; Naohiro Taniguchi; Shigehiko Miyamoto; Shin-ichiro Narita; Hajime Tokuda
Journal:  FEBS J       Date:  2007-05-17       Impact factor: 5.542

10.  The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis.

Authors:  J M Bolla; C Lazdunski; J M Pagès
Journal:  EMBO J       Date:  1988-11       Impact factor: 11.598

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  92 in total

1.  BamE modulates the Escherichia coli beta-barrel assembly machine component BamA.

Authors:  Nathan W Rigel; Jaclyn Schwalm; Dante P Ricci; Thomas J Silhavy
Journal:  J Bacteriol       Date:  2011-12-16       Impact factor: 3.490

Review 2.  The bacterial outer membrane β-barrel assembly machinery.

Authors:  Kelly H Kim; Suraaj Aulakh; Mark Paetzel
Journal:  Protein Sci       Date:  2012-05-01       Impact factor: 6.725

3.  Activation of the Escherichia coli β-barrel assembly machine (Bam) is required for essential components to interact properly with substrate.

Authors:  Dante P Ricci; Christine L Hagan; Daniel Kahne; Thomas J Silhavy
Journal:  Proc Natl Acad Sci U S A       Date:  2012-02-13       Impact factor: 11.205

4.  Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC.

Authors:  Chaille T Webb; Joel Selkrig; Andrew J Perry; Nicholas Noinaj; Susan K Buchanan; Trevor Lithgow
Journal:  J Mol Biol       Date:  2012-06-06       Impact factor: 5.469

Review 5.  Outer membrane protein biogenesis in Gram-negative bacteria.

Authors:  Sarah E Rollauer; Moloud A Sooreshjani; Nicholas Noinaj; Susan K Buchanan
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2015-10-05       Impact factor: 6.237

Review 6.  A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria.

Authors:  Karen G Fleming
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2015-10-05       Impact factor: 6.237

7.  The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain.

Authors:  Garner R Soltes; Jaclyn Schwalm; Dante P Ricci; Thomas J Silhavy
Journal:  J Bacteriol       Date:  2016-01-04       Impact factor: 3.490

8.  Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of Haemophilus influenzae BamD and BamCD complex.

Authors:  Jintang Lei; Xun Cai; Xiaodan Ma; Li Zhang; Yuwen Li; Xue Dong; Joseph St Geme; Guoyu Meng
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-01-28       Impact factor: 1.056

9.  Predicting functionally informative mutations in Escherichia coli BamA using evolutionary covariance analysis.

Authors:  Robert S Dwyer; Dante P Ricci; Lucy J Colwell; Thomas J Silhavy; Ned S Wingreen
Journal:  Genetics       Date:  2013-08-09       Impact factor: 4.562

10.  The major outer sheath protein (Msp) of Treponema denticola has a bipartite domain architecture and exists as periplasmic and outer membrane-spanning conformers.

Authors:  Arvind Anand; Amit Luthra; Maxwell E Edmond; Morgan Ledoyt; Melissa J Caimano; Justin D Radolf
Journal:  J Bacteriol       Date:  2013-03-01       Impact factor: 3.490

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