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Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment
Autotransporters are bacterial virulence factors consisting of an N-terminal “passenger domain” that is secreted in a C- to-N-terminal direction and a C-terminal “β domain” that resides in the outerExpand
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Sequential and spatially restricted interactions of assembly factors with an autotransporter β domain
Autotransporters are bacterial virulence factors that consist of an N-terminal extracellular (“passenger”) domain and a C-terminal β barrel domain (“β domain”) that resides in the outer membrane.Expand
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An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter.
Bacterial autotransporters are proteins that use a C-terminal porin-like domain to facilitate the transport of an upstream "passenger domain" across the outer membrane. Although autotransporters areExpand
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Basic Amino Acids in a Distinct Subset of Signal Peptides Promote Interaction with the Signal Recognition Particle*
Previous studies have demonstrated that signal peptides bind to the signal recognition particle (SRP) primarily via hydrophobic interactions with the 54-kDa protein subunit. The crystal structure ofExpand
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Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter
Bacterial autotransporters are proteins that contain a small C‐terminal ‘β domain’ that facilitates translocation of a large N‐terminal ‘passenger domain’ across the outer membrane (OM) by an unknownExpand
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Molecular basis for the activation of a catalytic asparagine residue in a self-cleaving bacterial autotransporter.
Autotransporters are secreted proteins produced by pathogenic Gram-negative bacteria. They consist of a membrane-embedded β-domain and an extracellular passenger domain that is sometimes cleaved andExpand
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An Unusual Signal Peptide Extension Inhibits the Binding of Bacterial Presecretory Proteins to the Signal Recognition Particle, Trigger Factor, and the SecYEG Complex*
Considerable evidence indicates that the Escherichia coli signal recognition particle (SRP) selectively targets proteins that contain highly hydrophobic signal peptides to the SecYEG complexExpand
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Mechanistic link between β barrel assembly and the initiation of autotransporter secretion
Significance Most proteins that reside in the bacterial outer membrane are β sheets that fold into a unique cylindrical structure known as a “β barrel.” Here we describe significant insights into theExpand
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Reconstitution of bacterial autotransporter assembly using purified components
Autotransporters are a superfamily of bacterial virulence factors consisting of an N-terminal extracellular (‘passenger’) domain and a C-terminal β barrel (‘β’) domain that resides in the outerExpand
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Folding of a bacterial integral outer membrane protein is initiated in the periplasm
The Bam complex promotes the insertion of β-barrel proteins into the bacterial outer membrane, but it is unclear whether it threads β-strands into the lipid bilayer in a stepwise fashion or catalyzesExpand
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