An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter

Szabady, Rose L.; Peterson, Janine H.; Skillman, Kristen M.; Bernstein, Harris

doi:10.1073/pnas.0406055102

Cited by 121 publications

(171 citation statements)

References 29 publications

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“…In this model, the expanded b-domain of Hbp would translocate the passenger domain while surrounded by the BamA oligomer. An expanded b-domain could be compatible with the observed translocation of small folded elements (Jong et al, 2007;Skillman et al, 2005). When translocation of the passenger is completed the Bam complex would disassemble, which might trigger the sealing of the bdomain and its folding into a stable barrel permitting the cleavage of the passenger domain.…”

Section: Discussionmentioning

confidence: 81%

“…Essentially, crystal structures of the b-domains of two ATs revealed a narrow 12-strand b-barrel pore structure with an inner diameter of 1.2 nm Oomen et al, 2004) that is incompatible with the reported secretion of small folded elements and closely spaced cysteine bridges engineered or naturally occurring in AT passenger domains Bodelon et al, 2009;Brandon & Goldberg, 2001;Jong et al, 2007;Oomen et al, 2004;Skillman et al, 2005). These incongruent data have led to discussions about the possible involvement of host factors in the OM translocation of ATs (Bernstein, 2007;Oomen et al, 2004).…”

Section: Discussionmentioning

confidence: 89%

“…Apparently, these interactions dissociate when translocation is complete. The transient nature of such contacts probably explains the reported inability to find interacting partners of fully assembled ATs in the OM (Muller et al, 2005;Skillman et al, 2005).…”

Section: Discussionmentioning

confidence: 98%

“…Passenger translocation is a very rapid process, meaning that putative contacts of the unprocessed AT (pro-Hbp) with external factors aiding in translocation are short-lived (Skillman et al, 2005). To improve the chances of identifying protein contacts between pro-Hbp and additional factors we made use of the paired cysteine mutant Hbp110C/348C.…”

Section: The Hbp110c/348c Translocation Intermediate Is Adjacent To Smentioning

confidence: 99%

“…1a, b). This 'classical' view of AT transport has recently been called into question as (i) crystal structures of b-domains Meng et al, 2006;Oomen et al, 2004) and molecular dynamics simulations (Khalid & Sansom, 2006) suggest that the pore formed by the bdomain only allows translocation of extended unfolded protein chains whereas various passengers can be translocated in a partially folded state (Jong et al, 2007;Skillman et al, 2005) and (ii) secretion of several ATs is significantly affected in cells depleted of BamA (or Omp85), the core component of the OM protein (OMP) assembly machinery (Jain & Goldberg, 2007;Voulhoux et al, 2003). Notably, BamA is homologous to the TpsB protein that acts as OM translocator in the 'two-partner secretion pathway', a secretion system related to the autotransporter pathway (Jacob-Dubuisson et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease

et al. 2009

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Autotransporters are large virulence factors secreted by Gram-negative bacteria. They are synthesized with a C-terminal domain that forms a b-barrel pore in the outer membrane implicated in translocation of the upstream 'passenger' domain across the outer membrane. However, recent structural data suggest that the diameter of the b-barrel pore is not sufficient to allow the passage of partly folded structures observed for several autotransporters. Here, we have used a stalled translocation intermediate of the autotransporter Hbp to identify components involved in insertion and translocation of the protein across the outer membrane. At this intermediate stage the b-domain was not inserted and folded as an integral b-barrel in the outer membrane whereas part of the passenger was surface exposed. The intermediate was copurified with the periplasmic chaperone SurA and subunits of the Bam (Omp85) complex that catalyse the insertion and assembly of outer-membrane proteins. The data suggest a critical role for this general machinery in the translocation of autotransporters across the outer membrane.

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Section: Discussionmentioning

confidence: 81%

Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 98%

Section: The Hbp110c/348c Translocation Intermediate Is Adjacent To Smentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease

et al. 2009

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Protein Secretion in Bacterial Cells

Stathopoulos

Yen

Tsang

et al. 2008

Bacterial Physiology

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Protein Folding in Bacterial Adhesion: Secretion and Folding of Classical Monomeric Autotransporters

Ulsen

2011

Advances in Experimental Medicine and Biology

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Bacterial adhesins mediate the attachment of bacteria to their niches, such as the tissue of an infected host. Adhesins have to be transported across the cell envelope to become active and during this secretion process they fold into their final conformation. This chapter focuses on the biogenesis of the classical monomeric autotransporter proteins, which are the most ubiquitous class of secreted proteins in Gram-negative bacteria. They may function as adhesins, but other functions are also known. Autotransporter proteins have a modular structure and consist of an N-terminal signal peptide and a C-terminal translocator domain with in between the secreted passenger domain that harbours the functions. The signal peptide directs the transport across the inner membrane to the periplasm via the Sec machinery. The translocator domain inserts into the outer membrane and facilitates the transport of the passenger to the cell surface. In this chapter, I will review our current knowledge of the secretion of classical monomeric autotransporters and the methods that have been used to assess their folding during the translocation, both in vitro and in vivo.

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An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter

Abstract: Escherichia coli ͉ microbial pathogenesis ͉ protein folding ͉ protein translocation

Cited by 121 publications

References 29 publications

The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease

The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease

Protein Secretion in Bacterial Cells

Protein Folding in Bacterial Adhesion: Secretion and Folding of Classical Monomeric Autotransporters

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