Crystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsA

Kühnel, Karin; Diezmann, Dagmar

doi:10.1128/jb.00790-10

Cited by 21 publications

(24 citation statements)

References 30 publications

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“…Stable cores have been reported in the C-terminal regions of three β-helical passengers (Junker et al, 2006; Kühnel and Diezmann, 2011; Renn and Clark, 2008) (Fig. 3).…”

Section: Back To the Passenger: What About More Specialized Terms: “Pmentioning

confidence: 86%

“…In many ATs the linker also includes a disordered region N-terminal to the α-helix. If the passenger is cleaved from the β-barrel after OM translocation, this cleavage site can be located within the linker and after OM translocation will be positioned either on the cell surface (Kühnel and Diezmann, 2011; Meng et al, 2011; Pohlner et al, 1987) or within the folded β-barrel structure (Dautin et al, 2007; Tajima et al, 2010). Some passengers have additional cleavage sites that separate different passenger domain structures after secretion (Fink et al, 2001; Nguyen et al, 2001; Ohnishi and Horinouchi, 1996; Pohlner et al, 1987).…”

Section: The Need For Unambiguous Definitions Of Common Autotransportmentioning

confidence: 99%

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Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion

Drobnak

Braselmann

Chaney

et al. 2014

Molecular Microbiology

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Autotransporter (AT) proteins provide a diverse array of important virulence functions to Gram-negative bacterial pathogens, and have also been adapted for protein surface display applications. The “autotransporter” moniker refers to early models that depicted these proteins facilitating their own translocation across the bacterial outer membrane. Although translocation is less autonomous than originally proposed, AT protein segments upstream of the C-terminal transmembrane β-barrel have nevertheless consistently been found to contribute to efficient translocation and/or folding of the N-terminal virulence region (the “passenger”). However, defining the precise secretion functions of these AT regions has been complicated by the use of multiple overlapping and ambiguous terms to define AT sequence, structural, and functional features, including “autochaperone”, “linker” and “junction”. Moreover, the precise definitions and boundaries of these features vary among ATs and even among research groups, leading to an overall murky picture of the contributions of specific features to translocation. Here we propose a unified, unambiguous nomenclature for AT structural, functional and conserved sequence features, based on explicit criteria. Applied to 16 well studied AT proteins, this nomenclature reveals new commonalities for translocation but also highlights that the autochaperone function is less closely coupled with a conserved sequence element than previously believed.

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“…Stable cores have been reported in the C-terminal regions of three β-helical passengers (Junker et al, 2006; Kühnel and Diezmann, 2011; Renn and Clark, 2008) (Fig. 3).…”

Section: Back To the Passenger: What About More Specialized Terms: “Pmentioning

confidence: 86%

Section: The Need For Unambiguous Definitions Of Common Autotransportmentioning

confidence: 99%

Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion

Drobnak

Braselmann

Chaney

et al. 2014

Molecular Microbiology

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“…Position 453 lies within the first predicted ␤-strand of the N-terminal extracellular domain (D00) of the passenger Thus, the introduced double HA tag presumably leads to misfolding of the D00 domain. Tsai et al (13) assumed that this domain could function as an autochaperone domain as it was described for classical monomeric autotransporters (31)(32)(33). Such domains initiate the vectorial export of the passenger by forming a hairpin intermediate and improve transport efficiency.…”

Section: Intha453 Is Expressed At the Wild Type Level And The ␤-Barrementioning

confidence: 99%

The Inverse Autotransporter Intimin Exports Its Passenger Domain via a Hairpin Intermediate

Oberhettinger

Leo

Linke

et al. 2015

Journal of Biological Chemistry

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Background:Intimin exports its C-terminal passenger domain through an N-terminal ␤-barrel onto the bacterial surface. Results: Insertion of an epitope tag at the very N terminus of the passenger domain stalls the export of the passenger. Conclusion:The intimin passenger adopts a hairpin conformation during translocation. Significance: Our results confirm the hairpin model of inverse autotransport where the passenger is translocated from the N to the C terminus.

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“…The autochaperone domain is required to trigger and ensure correct folding of the passenger domain to the bacterial surface. 113 The best-studied autotransporters in Shigella are IcsA, SepA, Pic and SigA. SepA, Pic and SigA belong to the SPATEs family.…”

Section: Do Not Distributementioning

confidence: 99%

Shigella

2012

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Crystal Structure of the Autochaperone Region from the Shigella flexneri Autotransporter IcsA

Cited by 21 publications

References 30 publications

Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion

Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion

The Inverse Autotransporter Intimin Exports Its Passenger Domain via a Hairpin Intermediate

Shigella

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