The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemi1 1Edited by I. B. Holland

Bouley, J.; Condemine, Guy; Shevchik, Vladimir E.

doi:10.1006/jmbi.2001.4594

Cited by 81 publications

(102 citation statements)

References 28 publications

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“…The second linker region, L2, located between the N-and the C-terminal domains, is 62-amino acids long and has a composition of 58% serine and glycine. A similar polyserine/glycine region has already been described for OutD and BfpB (16,37) and is also present in XpsD and TcpC secretins (Fig. 2).…”

Section: Hxcq Is a Member Of The Secretinsupporting

confidence: 77%

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HxcQ Liposecretin Is Self-piloted to the Outer Membrane by Its N-terminal Lipid Anchor

Viarre

Cascales

Ball

et al. 2009

Journal of Biological Chemistry

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Secretins are an unusual and important class of bacterial outer membrane (OM) proteins. They are involved in the transport of single proteins or macromolecular structures such as pili, needle complexes, and bacteriophages across the OM. Secretins are multimeric ring-shaped structures that form large pores in the OM. The targeting of such macromolecular structures to the OM often requires special assistance, conferred by specific pilotins or pilot proteins. Here, we investigated HxcQ, the OM component of the second Pseudomonas aeruginosa type II secretion system. We found that HxcQ forms high molecular mass structures resistant to heat and SDS, revealing its secretin nature. Interestingly, we showed that HxcQ is a lipoprotein. Construction of a recombinant nonlipidated HxcQ (HxcQnl) revealed that lipidation is essential for HxcQ function. Further phenotypic analysis indicated that HxcQnl accumulates as multimers in the inner membrane of P. aeruginosa, a typical phenotype observed for secretins in the absence of their cognate pilotin. Our observations led us to the conclusion that the lipid anchor of HxcQ plays a pilotin role. The self-piloting of HxcQ to the OM was further confirmed by its correct multimeric OM localization when expressed in the heterologous host Escherichia coli. Altogether, our results reveal an original and unprecedented pathway for secretin transport to the OM.

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Section: Hxcq Is a Member Of The Secretinsupporting

confidence: 77%

“…2) (15). Therefore, this domain has been proposed to form the secretion channel, whereas the much less conserved N-terminal domain that largely protrudes into the periplasm probably undertakes more specific functions, such as substrate recognition and/or interaction with the other components of the corresponding machineries (13,16).…”

mentioning

confidence: 99%

HxcQ Liposecretin Is Self-piloted to the Outer Membrane by Its N-terminal Lipid Anchor

Viarre

Cascales

Ball

et al. 2009

Journal of Biological Chemistry

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“…The majority of the components of T2SS are highly conserved, and most of the corresponding genes can be swapped between diverse bacterial species, except for gspC and gspD (3,4) (gsp for general secretory pathway (5)). The T2SS of the phytopathogenic enterobacteria Erwinia chrysanthemi, referred to as the Out system, secretes several pectinases and a cellulase (6).…”

Section: The Type II Secretion System (T2ss)mentioning

confidence: 99%

“…The existence of two separate steps in the T2S pathway assumes that the secreted proteins, once they have been exported into the periplasm, should be recognized by a special element(s) of the T2S machinery. The inner membrane protein OutC has been suggested for the roles of signal transduction between the two cell membranes and recognition of secreted proteins (3,6,7,9).…”

Section: The Type II Secretion System (T2ss)mentioning

confidence: 99%

“…Some algorithms also predict a coiled-coil structure for Erwinia OutC. Regardless of its structure, inter-species swapping indicated that this region of OutC directly participates in the specific recognition of the secreted proteins (6). Recently it was proposed that this region of GspC could be involved in the formation of homo-multimeric complexes (13).…”

Section: The Type II Secretion System (T2ss)mentioning

confidence: 99%

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The Single Transmembrane Segment Drives Self-assembly of OutC and the Formation of a Functional Type II Secretion System in Erwinia chrysanthemi

Shevchik

2006

Journal of Biological Chemistry

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Many pathogenic Gram-negative bacteria secrete toxins and lytic enzymes via a multiprotein complex called the type II secretion system. This system, named Out in Erwinia chrysanthemi, consists of 14 proteins integrated or associated with the two bacterial membranes. OutC, a key player in this process, is probably implicated in the recognition of secreted proteins and signal transduction. OutC possesses a short cytoplasmic sequence, a single transmembrane segment (TMS), and a large periplasmic region carrying a putative PDZ domain. A hydrodynamic study revealed that OutC forms stable dimers of an elongated shape, whereas the PDZ domain adopts a globular shape. Bacterial two-hybrid, crosslinking, and pulldown assays revealed that the self-association of OutC is driven by the TMS, whereas the periplasmic region is dispensable for self-association. Site-directed mutagenesis of the TMS revealed that cooperative interactions between three polar residues located at the same helical face provide adequate stability for OutC self-assembly. An interhelical H-bonding mediated by Gln 29 appears to be the main driving force, and two Arg residues located at the TMS boundaries are essential for the stabilization of OutC oligomers. Stepwise mutagenesis of these residues gradually diminished OutC functionality and self-association ability. The triple OutC mutant R15V/Q29L/R36A became monomeric and nonfunctional. Self-association and functionality of the triple mutant were partially restored by the introduction of a polar residue at an alternative position in the interhelical interface. Thus, the OutC TMS is more than just a membrane anchor; it drives the protein self-association that is essential for formation of a functional secretion system.

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The secretome of the plant pathogenic bacterium Erwinia chrysanthemi

Kazemipour

Condemine

Hugouvieux‐Cotte‐Pattat

2004

Proteomics

172

143

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Erwinia chrysanthemi causes soft-rot diseases of many plants by secreting a battery of enzymes which degrade the plant cell walls. We initiated a proteomic analysis to create a reference map of the E. chrysanthemi secretome. Extracellular proteins were isolated from E. chrysanthemi culture supernatants and resolved by two-dimensional electrophoresis. By analysis of mutants, Western blotting, and matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) 55 spots representing 25 unique proteins were identified. In uninduced conditions, we identified spots corresponding to the cellulase Cel5, the proteases PrtA, PrtB, and PrtC, the flagellin FliC, and some intracellular proteins whose presence probably resulted from spontaneous cell lysis. We identified another secreted protein, AvrL, homologous to an avirulence protein of Xanthomonas campestris. After culture in conditions inducing pectinase production, i.e., in the presence of galacturonate and plant extract, we identified spots corresponding to the endopectate lyases PelA, PelB, PelC, PelD, PelE, PelI, PelL, and PelZ, the pectin acetylesterases PaeX and PaeY, the pectin methylesterase PemA, and the polygalacturonase PehX. In the presence of other inducing compounds, we detected the rhamnogalacturonate lyase RhiE and the esterase FaeD. Analysis of mutants, altered for one type of secretion system, was performed to determine the targets of each system. The type I system Prt was necessary for the secretion of three proteases. No proteins secreted by the type III Hrp system could be detected in E. chrysanthemi supernatants. In addition to the already known substrates (eleven pectinases and one cellulase), this analysis revealed that the type II Out system mediates secretion of the esterase FaeD and of the Avr-like protein AvrL.

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The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemi1 1Edited by I. B. Holland

Cited by 81 publications

References 28 publications

HxcQ Liposecretin Is Self-piloted to the Outer Membrane by Its N-terminal Lipid Anchor

HxcQ Liposecretin Is Self-piloted to the Outer Membrane by Its N-terminal Lipid Anchor

The Single Transmembrane Segment Drives Self-assembly of OutC and the Formation of a Functional Type II Secretion System in Erwinia chrysanthemi

The secretome of the plant pathogenic bacterium Erwinia chrysanthemi

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