C‐terminal specific protein degradation: Activity and substrate specificity of the Tsp protease

Keiler, Kenneth C.; Silber, Karen R.; Downard, Kevin M.; Papayannopoulos, Ioannis A.; Biemann, K.; Sauer, Robert T.

doi:10.1002/pro.5560040808

Cited by 73 publications

(87 citation statements)

References 30 publications

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“…SecA is an ATPase motor that binds to the inner membrane SecYEG channel to form the essential protein translocase core (39). Tsp and DegQ are periplasmic serine proteases (29)(30)(31)(32)(33)(34)(35)(36)(37). TogA is the ATPase subunit of the ABC transporter that imports oligogalacturonides (24).…”

Section: Resultsmentioning

confidence: 99%

Erwinia chrysanthemiIron Metabolism: the Unexpected Implication of the Inner Membrane Platform within the Type II Secretion System

Douet¹,

Expert

Barras³

et al. 2009

J Bacteriol

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The type II secretion (T2S) system is an essential device for Erwinia chrysanthemi virulence. Previously, we reported the key role of the OutF protein in forming, along with OutELM, an inner membrane platform in the Out T2S system. Here, we report that OutF copurified with five proteins identified by matrix-assisted laser desorption ionization-time of flight analysis as AcsD, TogA, SecA, Tsp, and DegP. The AcsD protein was known to be involved in the biosynthesis of achromobactin, which is a siderophore important for E. chrysanthemi virulence. The yeast two-hybrid system allowed us to gain further evidence for the OutF-AcsD interaction. Moreover, we showed that lack of OutF produced a pleiotropic phenotype: (i) altered production of the two siderophores of E. chrysanthemi, achromobactin and chrysobactin; (ii) hypersensitivity to streptonigrin, an iron-activated antibiotic; (iii) increased sensitivity to oxidative stress; and (iv) absence of the FbpA-like iron-binding protein in the periplasmic fraction. Interestingly, outE and outL mutants also exhibited similar phenotypes, but, outD and outJ mutants did not. Moreover, using the yeast two-hybrid system, several interactions were shown to occur between components of the T2S system inner membrane platform (OutEFL) and proteins involved in achromobactin production (AcsABCDE). The OutL-AcsD interaction was also demonstrated by Ni 2؉ affinity chromatography. These results fully confirm our previous view that the T2S machinery is made up of three discrete blocks. The OutEFLM-forming platform is proposed to be instrumental in two different processes essential for virulence, protein secretion and iron homeostasis.Pathogenicity is a multifactorial process that includes virulence factors that act directly on the target and general metabolic functions that ensure adaptation of the pathogen to its host environment. The enterobacterium Erwinia chrysanthemi causes the so-called soft-rot disease of almost all dicotyledons it has been tested on (40,58). This disease is responsible for severe losses in harvests of many plants, such as potatoes, chicories, and ornamental flowers. E. chrysanthemi-caused soft-rot disease is therefore an issue of great economic importance.Major virulence factors produced by E. chrysanthemi include a series of secreted plant cell wall-degrading enzymes, such as pectinases (pectate lyases, pectin methyl esterases, and polygalacturonases) and cellulases (4, 28). Most of these extracellular enzymes are secreted by the type II secretion (T2S) system, referred to as Out in E. chrysanthemi. Accordingly, out mutants are nonpathogenic, underscoring the major role of the T2S system in E. chrysanthemi virulence (1). T2S systems have been identified in a wide variety of Proteobacteria and are composed of over 10 proteins that presumably form a trans-envelope complex (11,27,50). The E. chrysanthemi Out T2S system is made up of 14 proteins. Two of them, OutD and OutS, are located in the outer membrane and are thought to form the exit pore (54, 55). Four Out prote...

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Section: Resultsmentioning

confidence: 99%

Erwinia chrysanthemiIron Metabolism: the Unexpected Implication of the Inner Membrane Platform within the Type II Secretion System

Douet¹,

Expert

Barras³

et al. 2009

J Bacteriol

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“…The mechanism by which NSR confers resistance is proposed to involve the proteolytic degradation of nisin, mediated by a C-terminally conserved, tail-specific protease (TSPc) domain (184,185). TSPc-containing enzymes efficiently cleave substrates that have apolar residues and a free alpha-carboxylate at the C terminus and have been identified and characterized in a range of species, including E. coli (186). Such proteases contain a conserved PDZ domain adjacent to the TSPc domain, which is indispensable for binding of the TSPc domain to nonpolar C termini of its peptide substrates and thus for the catalytic activity (187,188).…”

Section: Nisin Resistance Proteinmentioning

confidence: 99%

Lantibiotic Resistance

Draper

Cotter

Hill

et al. 2015

Microbiol Mol Biol Rev

135

129

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SUMMARY The dramatic rise in the incidence of antibiotic resistance demands that new therapeutic options will have to be developed. One potentially interesting class of antimicrobials are the modified bacteriocins termed lantibiotics, which are bacterially produced, posttranslationally modified, lanthionine/methyllanthionine-containing peptides. It is interesting that low levels of resistance have been reported for lantibiotics compared with commercial antibiotics. Given that there are very few examples of naturally occurring lantibiotic resistance, attempts have been made to deliberately induce resistance phenotypes in order to investigate this phenomenon. Mechanisms that hinder the action of lantibiotics are often innate systems that react to the presence of any cationic peptides/proteins or ones which result from cell well damage, rather than being lantibiotic specific. Such resistance mechanisms often arise due to altered gene regulation following detection of antimicrobials/cell wall damage by sensory proteins at the membrane. This facilitates alterations to the cell wall or changes in the composition of the membrane. Other general forms of resistance include the formation of spores or biofilms, which are a common mechanistic response to many classes of antimicrobials. In rare cases, bacteria have been shown to possess specific antilantibiotic mechanisms. These are often species specific and include the nisin lytic protein nisinase and the phenomenon of immune mimicry.

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“…However, the role of Prc in the pathogenesis of E. coli infection remains to be elucidated. Prc, originally identified in E. coli as a periplasmic protease, has been shown to be responsible for the C-terminal processing of a periplasmic protein, penicillin-binding protein 3 (PBP-3), in E. coli and to selectively degrade proteins with nonpolar C termini in vitro (16,21,22,37). In addition, E. coli with an inactivated prc gene exhibits periplasmic protein leakage suggestive of increased outer membrane (OM) permeability (16), which may be responsible for the mutant's growth defect under conditions of osmotic stress (low osmolarity) at 42°C and its increased susceptibility to multiple antibiotics (16,36).…”

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confidence: 99%

Prc Contributes to Escherichia coli Evasion of Classical Complement-Mediated Serum Killing

Wang

Huang

et al. 2012

Infect Immun

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ABSTRACTEscherichia coliis a common Gram-negative organism that causes bacteremia. Prc, a bacterial periplasmic protease, and its homologues are known to be involved in the pathogenesis of Gram-negative bacterial infections. The present study examined the role of Prc inE. colibacteremia and characterized the ability of theprcmutant of the pathogenicE. colistrain RS218 to cause bacteremia and survive in human serum. Theprcmutant of RS218 exhibited a decreased ability to cause a high level of bacteremia and was more sensitive to serum killing than strain RS218. This sensitivity was due to the mutant's decreased ability to avoid the activation of the antibody-dependent and -independent classical complement cascades as well as its decreased resistance to killing mediated by the membrane attack complex, the end product of complement system activation. The demonstration of Prc in the evasion of classical complement-mediated serum killing of pathogenicE. colimakes this factor a potential target for the development of therapeutic and preventive measures againstE. colibacteremia.

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C‐terminal specific protein degradation: Activity and substrate specificity of the Tsp protease

Cited by 73 publications

References 30 publications

Erwinia chrysanthemiIron Metabolism: the Unexpected Implication of the Inner Membrane Platform within the Type II Secretion System

Erwinia chrysanthemiIron Metabolism: the Unexpected Implication of the Inner Membrane Platform within the Type II Secretion System

Lantibiotic Resistance

Prc Contributes to Escherichia coli Evasion of Classical Complement-Mediated Serum Killing

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