ArticleJournal of bacteriology2011
Residues in a conserved α-helical segment are required for cleavage but not secretion of an Escherichia coli serine protease autotransporter passenger domain.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Comparative antibacterial activity of N-terminal and C-terminal domains of a recombinant endolysin againstApplied and environmental microbiology · 2025Article
- BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.Molecular cell · 2021Article
- Serine Protease Autotransporters of theMicroorganisms · 2019Review
- TleA, a Tsh-like autotransporter identified in a human enterotoxigenic Escherichia coli strain.Infection and immunity · 2015Article
- Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015Review
- Stepwise folding of an autotransporter passenger domain is not essential for its secretion.The Journal of biological chemistry · 2013Article
- Review
- Single-cell characterization of autotransporter-mediated Escherichia coli surface display of disulfide bond-containing proteins.The Journal of biological chemistry · 2012Article
- From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis.Nature reviews. Microbiology · 2012Review
- IcsA autotransporter passenger promotes increased fusion protein expression on the cell surface.Microbial cell factories · 2012Article
- Molecular basis for the activation of a catalytic asparagine residue in a self-cleaving bacterial autotransporter.Journal of molecular biology · 2012Article
- A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters.PloS one · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Autotransporters are a superfamily of virulence factors produced by Gram-negative bacteria that are comprised of an N-terminal extracellular domain (passenger domain) and a C-terminal β barrel domain (β domain) that resides in the outer membrane (OM). The β domain promotes the translocation of the passenger domain across the OM by an unknown mechanism. Available evidence indicates that an α-helical segment that spans the passenger domain-β domain junction is embedded inside the β domain at an early stage of assembly. Following its secretion, the passenger domain of the serine protease autotransporters of the Enterobacteriaceae (SPATEs) and the pertactin family of Bordetella pertussis autotransporters is released from the β domain through an intrabarrel autoproteolytic cleavage of the α-helical segment. Although the mutation of conserved residues that surround the cleavage site has been reported to impair both the translocation and cleavage of the passenger domain of a SPATE called Tsh, we show here that the mutation of the same residues in another SPATE (EspP) affects only passenger domain cleavage. Our results strongly suggest that the conserved residues are required to position the α-helical segment for the cleavage reaction and are not required to promote passenger domain secretion.
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