Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli

Gawarzewski, Iris; DiMaio, Frank; Winterer, Elisa; Tschapek, Britta; Smits, Sander H. J.; Jose, Joachim; Schmitt, Lutz

doi:10.1016/j.jsb.2014.05.003

Cited by 32 publications

(21 citation statements)

References 54 publications

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“…Inclusion of an autochaperone is predicated on it being experimentally shown to rescue folding-deficient passenger mutants when supplied in trans . Translocators correspond to the minimal units required to secrete a passenger, typically a heterologous one. a Charles et al (1989); Emsley et al (1996); Junker et al (2009, 2006); Makoff et al (1990) b Oliver et al (2003a,b); Zhai et al (2011) c Barnard et al (2007, 2012); Brockmeyer et al (2009); Dutta et al (2003); Khan et al (2011); Skillman et al (2005); Szabady et al (2005); Velarde and Nataro (2004) d Otto et al (2005); Saurí et al (2011); Soprova et al (2010); Tajima et al (2010) e Dutta et al (2003); Meza-Aguilar et al (2014); Renn et al (2012); Renn and Clark (2008) f Fink et al (2001); Meng et al (2011) g Johnson et al (2009); Klauser et al (1993, 1990); Pohlner et al (1987, 1995); van Ulsen et al (2003) h Côté and Mourez (2011); Lindenthal and Elsinghorst (1999) i Brandon and Goldberg (2001); Kühnel and Diezmann (2011); May and Morona (2008); Suzuki et al (1995); Teh and Morona (2013) j Heras et al (2014); Ramesh et al (2012); van der Woude and Henderson (2008) k Benz and Schmidt (1992); Berthiaume et al (2007); Charbonneau et al (2006); Charbonneau and Mourez (2007); Gawarzewski et al (2014); Maurer et al (1999); Rutherford et al (2006); Suhr et al (1996) l Besingi et al (2013) m van den Berg (2010); Wilhelm et al (2007, 199...…”

Section: Figurementioning

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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Section: Figurementioning

confidence: 99%

“… k Benz and Schmidt (1992); Berthiaume et al (2007); Charbonneau et al (2006); Charbonneau and Mourez (2007); Gawarzewski et al (2014); Maurer et al (1999); Rutherford et al (2006); Suhr et al (1996) …”

Section: Figurementioning

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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“…Passenger domains typically fold into an unusual repetitive structure known as a β helix and often mediate a virulence function in pathogenic bacteria. Although the sequence of the C‐terminal domains are highly divergent, they fold into nearly superimposable 12‐stranded β barrels (Oomen et al, ; Barnard et al, ; van den Berg, ; Zhai et al, ; Gawarzewski et al, ). Several reliable assays can be used to monitor discrete stages of autotransporter assembly in vivo.…”

Section: Introductionmentioning

confidence: 99%

Identification of a novel post‐insertion step in the assembly of a bacterial outer membrane protein

Peterson

Hussain

Bernstein

2018

Molecular Microbiology

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Although the barrel assembly machinery (Bam) complex has been shown to facilitate the insertion of β barrel proteins into the bacterial outer membrane (OM), the stage at which β barrels fold is unknown. Here, we describe insights into β barrel assembly that emerged from an analysis of a member of the autotransporter family of OM proteins (EspP) in Escherichia coli. EspP contains an extracellular 'passenger' domain that is translocated across the OM and then released from the covalently linked β barrel domain in an intra-barrel cleavage reaction. We found that the mutation of an unusual lipid-exposed lysine residue impairs a previously unidentified late folding step that follows both the membrane insertion of the β barrel domain and the secretion of the passenger domain but that precedes proteolytic maturation. Our results demonstrate that β barrel assembly can be completed at a post-insertion stage and raise the possibility that interactions with membrane lipids can promote folding in vivo. Furthermore, by showing that the passenger domain is secreted before the β barrel domain is fully assembled, our results also provide evidence against the long-standing hypothesis that autotransporters are autonomous protein secretion systems.

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“…Furthermore it allows, after transport of an apoprotein to the cell surface, the incorporation of prosthetic groups or cofactors without disturbing cell integrity or cell viability (Schumacher et al, ). The translocation mechanism was enlightened recently (Gawarzewski et al, ; Pavlova et al, ). The Autodisplay system was already successfully used for the utilization of, for example, hyaluronidases (Kaessler et al, ), lipases (Kranen et al, ), as well as nitrilases (Detzel et al, , ).…”

Section: Introductionmentioning

confidence: 99%

A simplified process design for P450 driven hydroxylation based on surface displayed enzymes

Ströhle

Kranen²,

Schrader

et al. 2015

Biotech & Bioengineering

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New production routes for fine and bulk chemicals are important to establish further sustainable processes in industry. Besides the identification of new biocatalysts and new production routes the optimization of existing processes in regard to an improved utilization of the catalysts are needed. In this paper we describe the successful expression of P450BM3 on the surface of E. coli cells with the Autodisplay system. The successful hydroxylation of palmitic acid by using surface-displayed P450BM3 was shown. Besides optimization of surface protein expression, several cofactor regeneration systems were compared and evaluated. Afterwards, the development of a suitable process for the biocatalytic hydroxylation of fatty acids based on the re-use of the catalysts after a simple centrifugation was investigated. It was shown that the catalyst can be used for several times without any loss in activity. By using surface-displayed P450s in combination with an enzymatic cofactor regeneration system a total turnover number of up to 54,700 could be reached, to the knowledge of the authors the highest value reported for a P450 monooxygenase to date. Further optimizations of the described reaction system can have an enormous impact on the process design for more sustainable bioprocesses. Biotechnol. Bioeng. 2016;113: 1225-1233. © 2015 Wiley Periodicals, Inc.

show abstract

Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli

Cited by 32 publications

References 54 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

Identification of a novel post‐insertion step in the assembly of a bacterial outer membrane protein

A simplified process design for P450 driven hydroxylation based on surface displayed enzymes

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