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

Oberhettinger, Philipp; Leo, Jack C.; Linke, Dirk; Autenrieth, Ingo B.; Schütz, Monika

doi:10.1074/jbc.m114.604769

Cited by 31 publications

(46 citation statements)

References 50 publications

(19 reference statements)

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“…The C-terminus was in turn stained with antibodies only upon permeabilization of cells with detergent. This strongly suggests the presence of a hairpin-like conformation of the stalled translocation intermediate (105).…”

Section: Insertional Mutagenesis and Point Mutationsmentioning

confidence: 83%

“…The TpsB proteins are homologous to BamA, the central component of a multiprotein complex, the βbarrel assembly machinery or Bam complex, responsible for the insertion of all transmembrane β-barrel proteins into the outer membrane (99,100). Because BamA has been implicated in the biogenesis of autotransporter proteins (25,(101)(102)(103)(104)(105), we include a short discussion on the structure of this protein. Like FhaC, BamA consists of a 16-stranded β-barrel (106)(107)(108) (Fig.…”

Section: Translocation Domainsmentioning

confidence: 99%

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Type V Secretion Systems in Bacteria

et al. 2016

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Type V secretion denotes a variety of secretion systems that cross the outer membrane in Gram-negative bacteria but that depend on the Sec machinery for transport through the inner membrane. They are possibly the simplest bacterial secretion systems, because they consist only of a single polypeptide chain (or two chains in the case of two-partner secretion). Their seemingly autonomous transport through the outer membrane has led to the term "autotransporters" for various subclasses of type V secretion. In this chapter, we review the structure and function of these transporters and review recent findings on additional factors involved in the secretion process, which have put the term "autotransporter" to debate.

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Section: Insertional Mutagenesis and Point Mutationsmentioning

confidence: 83%

Section: Translocation Domainsmentioning

confidence: 99%

Type V Secretion Systems in Bacteria

et al. 2016

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“…Preparation of outer membranes was carried out as described previously48. Briefly, 50 ml of bacterial culture were harvested, re-suspended in 500 μl of resuspension buffer containing 500 μg lysozyme.…”

Section: Methodsmentioning

confidence: 99%

Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins

Pfitzner

Steblau

Ulrich

et al. 2016

Sci Rep

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β-Barrel proteins are found in the outer membrane (OM) of Gram-negative bacteria, chloroplasts and mitochondria. The assembly of these proteins into the corresponding OM is facilitated by a dedicated protein complex that contains a central conserved β-barrel protein termed BamA in bacteria and Tob55/Sam50 in mitochondria. BamA and Tob55 consist of a membrane-integral C-terminal domain that forms a β-barrel pore and a soluble N-terminal portion comprised of one (in Tob55) or five (in BamA) polypeptide transport-associated (POTRA) domains. Currently the functional significance of this difference and whether the homology between BamA and Tob55 can allow them to replace each other are unclear. To address these issues we constructed hybrid Tob55/BamA proteins with differently configured N-terminal POTRA domains. We observed that constructs harboring a heterologous C-terminal domain could not functionally replace the bacterial BamA or the mitochondrial Tob55 demonstrating species-specific requirements. Interestingly, the various hybrid proteins in combination with the bacterial chaperones Skp or SurA supported to a variable extent the assembly of bacterial β-barrel proteins into the mitochondrial OM. Collectively, our findings suggest that the membrane assembly of various β-barrel proteins depends to a different extent on POTRA domains and periplasmic chaperones.

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“…BamA is crucial for the correct insertion of most OMPs with deletion of the gene leading to a lethal phenotype [22]. This is further highlighted by the fact that the BAM complex is responsible for the insertion of all transmembrane pore domains of type V secretion systems [8] with BamA as the central component in autotransporter biogenesis for trimeric autotransporters [23]. In the case of TAAs, trimerization of the β-barrel seems to occur in the periplasm [24].…”

Section: Insertion and Folding Of Taas Into The Outer Membrane Of Gramentioning

confidence: 99%

Recent advances in the understanding of trimeric autotransporter adhesins

Kießling

Malik

Goldman

2019

Med Microbiol Immunol

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Adhesion is the initial step in the infection process of gram-negative bacteria. It is usually followed by the formation of biofilms that serve as a hub for further spread of the infection. Type V secretion systems engage in this process by binding to components of the extracellular matrix, which is the first step in the infection process. At the same time they provide protection from the immune system by either binding components of the innate immune system or by establishing a physical layer against aggressors. Trimeric autotransporter adhesins (TAAs) are of particular interest in this family of proteins as they possess a unique structural composition which arises from constraints during translocation. The sequence of individual domains can vary dramatically while the overall structure can be very similar to one another. This patchwork approach allows researchers to draw conclusions of the underlying function of a specific domain in a structure-based approach which underscores the importance of solving structures of yet uncharacterized TAAs and their individual domains to estimate the full extent of functions of the protein a priori. Here, we describe recent advances in understanding the translocation process of TAAs and give an overview of structural motifs that are unique to this class of proteins. The role of BpaC in the infection process of Burkholderia pseudomallei is highlighted as an exceptional example of a TAA being at the centre of infection initiation.

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

Cited by 31 publications

References 50 publications

Type V Secretion Systems in Bacteria

Type V Secretion Systems in Bacteria

Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins

Recent advances in the understanding of trimeric autotransporter adhesins

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