Literature DB >> 21823654

The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of β-barrel assembly.

Christine L Hagan1, Daniel Kahne.   

Abstract

β-Barrel proteins are folded and inserted into the outer membranes of Escherichia coli by the Bam complex. The Bam complex has been purified and functionally reconstituted in vitro. We report conditions for reconstitution that increase the folding yield 10-fold and allow us to monitor the time course of folding directly. We use these conditions to analyze the effect of a mutation in the Bam complex and to demonstrate the ability of the reconstituted complex to catalyze more than one round of substrate assembly.

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Year:  2011        PMID: 21823654      PMCID: PMC3192448          DOI: 10.1021/bi2010784

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  30 in total

1.  The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex.

Authors:  Nicholas Noinaj; James W Fairman; Susan K Buchanan
Journal:  J Mol Biol       Date:  2011-01-26       Impact factor: 5.469

2.  Crystal structure of Escherichia coli BamB, a lipoprotein component of the β-barrel assembly machinery complex.

Authors:  Kelly H Kim; Mark Paetzel
Journal:  J Mol Biol       Date:  2010-12-17       Impact factor: 5.469

Review 3.  Protein translocation across the bacterial cytoplasmic membrane.

Authors:  Arnold J M Driessen; Nico Nouwen
Journal:  Annu Rev Biochem       Date:  2008       Impact factor: 23.643

4.  Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes.

Authors:  Timothy J Knowles; Mark Jeeves; Saeeda Bobat; Felician Dancea; Darren McClelland; Tracy Palmer; Michael Overduin; Ian R Henderson
Journal:  Mol Microbiol       Date:  2008-04-21       Impact factor: 3.501

Review 5.  Augmenting β-augmentation: structural basis of how BamB binds BamA and may support folding of outer membrane proteins.

Authors:  Alexander Heuck; Alexander Schleiffer; Tim Clausen
Journal:  J Mol Biol       Date:  2011-01-12       Impact factor: 5.469

6.  Structural characterization of Escherichia coli BamE, a lipoprotein component of the β-barrel assembly machinery complex.

Authors:  Kelly H Kim; Hyun-Seo Kang; Mark Okon; Eric Escobar-Cabrera; Lawrence P McIntosh; Mark Paetzel
Journal:  Biochemistry       Date:  2011-01-24       Impact factor: 3.162

7.  Reconstitution of outer membrane protein assembly from purified components.

Authors:  Christine L Hagan; Seokhee Kim; Daniel Kahne
Journal:  Science       Date:  2010-04-08       Impact factor: 47.728

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.  Structure and function of BamE within the outer membrane and the β-barrel assembly machine.

Authors:  Timothy J Knowles; Douglas F Browning; Mark Jeeves; Riyaz Maderbocus; Sandya Rajesh; Pooja Sridhar; Eleni Manoli; Danielle Emery; Ulf Sommer; Ashley Spencer; Denisse L Leyton; Derrick Squire; Roy R Chaudhuri; Mark R Viant; Adam F Cunningham; Ian R Henderson; Michael Overduin
Journal:  EMBO Rep       Date:  2011-01-07       Impact factor: 8.807

10.  Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane.

Authors:  Petia Zvezdanova Gatzeva-Topalova; Lisa Rosa Warner; Arthur Pardi; Marcelo Carlos Sousa
Journal:  Structure       Date:  2010-11-10       Impact factor: 5.006

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  34 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

5.  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

6.  Putative vaccine candidates and drug targets identified by reverse vaccinology and subtractive genomics approaches to control Haemophilus ducreyi, the causative agent of chancroid.

Authors:  Alissa de Sarom; Arun Kumar Jaiswal; Sandeep Tiwari; Letícia de Castro Oliveira; Debmalya Barh; Vasco Azevedo; Carlo Jose Oliveira; Siomar de Castro Soares
Journal:  J R Soc Interface       Date:  2018-05       Impact factor: 4.118

7.  Inhibition of the β-barrel assembly machine by a peptide that binds BamD.

Authors:  Christine L Hagan; Joseph S Wzorek; Daniel Kahne
Journal:  Proc Natl Acad Sci U S A       Date:  2015-02-02       Impact factor: 11.205

8.  Inhibitor of intramembrane protease RseP blocks the σE response causing lethal accumulation of unfolded outer membrane proteins.

Authors:  Anna Konovalova; Marcin Grabowicz; Carl J Balibar; Juliana C Malinverni; Ronald E Painter; Daniel Riley; Paul A Mann; Hao Wang; Charles G Garlisi; Brad Sherborne; Nathan W Rigel; Dante P Ricci; Todd A Black; Terry Roemer; Thomas J Silhavy; Scott S Walker
Journal:  Proc Natl Acad Sci U S A       Date:  2018-06-25       Impact factor: 11.205

9.  Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA.

Authors:  Dennis Gessmann; Yong Hee Chung; Emily J Danoff; Ashlee M Plummer; Clifford W Sandlin; Nathan R Zaccai; Karen G Fleming
Journal:  Proc Natl Acad Sci U S A       Date:  2014-04-08       Impact factor: 11.205

Review 10.  From Chaperones to the Membrane with a BAM!

Authors:  Ashlee M Plummer; Karen G Fleming
Journal:  Trends Biochem Sci       Date:  2016-07-19       Impact factor: 13.807

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