Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli

Drew Bennion, Emily S. Charlson, Eric Coon, Rajeev Misra

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80 Citations (Scopus)

Abstract

BamA of Escherichia coli is an essential component of the hetero-oligomeric machinery that mediates β-barrel outer membrane protein (OMP) assembly. The C- and N-termini of BamA fold into trans-membrane β-barrel and five soluble POTRA domains respectively. Detailed characterization of BamA POTRA 1 missense and deletion mutants revealed two competing OMP assembly pathways, one of which is followed by the archetypal trimeric β-barrel OMPs, OmpF and LamB, and is dependent on POTRA 1. Interestingly, our data suggest that BamA also requires its POTRA 1 domain for proper assembly. The second pathway is independent of POTRA 1 and is exemplified by TolC. Site-specific cross-linking analysis revealed that the POTRA 1 domain of BamA interacts with SurA, a periplasmic chaperone required for the assembly of OmpF and LamB, but not that of TolC and BamA. The data suggest that SurA and BamA POTRA 1 domain function in concert to assist folding and assembly of most β-barrel OMPs except for TolC, which folds into a unique soluble α-helical barrel and an OM-anchored β-barrel. The two assembly pathways finally merge at some step beyond POTRA 1 but presumably before membrane insertion, which is thought to be catalysed by the trans-membrane β-barrel domain of BamA.

Original languageEnglish (US)
Pages (from-to)1153-1171
Number of pages19
JournalMolecular Microbiology
Volume77
Issue number5
DOIs
StatePublished - Sep 2010

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  • Molecular Biology
  • Microbiology

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Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli. / Bennion, Drew; Charlson, Emily S.; Coon, Eric; Misra, Rajeev.

In: Molecular Microbiology, Vol. 77, No. 5, 09.2010, p. 1153-1171.

Research output: Contribution to journalArticle

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