TldD/TldE peptidases and N-deacetylases: A structurally unique yet ubiquitous protein family in the microbial metabolism

Vobruba, Šimon; Kadlčík, Stanislav; Janata, Jiřı́; Kameník, Zdeněk

doi:10.1016/j.micres.2022.127186

Cited by 4 publications

(4 citation statements)

References 71 publications

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“…Once again, the cognate proteases are not encoded in the BGCs of these compounds. Consistent with this observation, TldD/E proteases are not only involved in the production of RiPPs but are believed to often have multiple other cellular functions . As a clear demonstration of the non-sequence-dependent substrate recognition, the TldD/E involved in microcin B17 biosynthesis was also able to remove the leader peptides from klebsazolicin and McC Yps despite very diverse sequences. , …”

Section: Metalloproteasesmentioning

confidence: 60%

“…Consistent with this observation, TldD/E proteases are not only involved in the production of RiPPs but are believed to often have multiple other cellular functions. 135 As a clear demonstration of the non-sequence-dependent substrate recognition, the TldD/E involved in microcin B17 biosynthesis was also able to remove the leader peptides from klebsazolicin and McC Yps despite very diverse sequences. 134,136 The currently characterized BGCs of the pearlin RiPP class encode either TldD/E-like or M50 family proteases.…”

Section: ■ Metalloproteasesmentioning

confidence: 99%

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Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis

Eslami,

van der Donk

2023

ACS Bio Med Chem Au

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Ribosomally synthesized and post-translationally modified peptides (RiPPs) have received much attention in recent years because of their promising bioactivities and the portability of their biosynthetic pathways. Heterologous expression studies of RiPP biosynthetic enzymes identified by genome mining often leave a leader peptide on the final product to prevent toxicity to the host and to allow the attachment of a genetically encoded affinity purification tag. Removal of the leader peptide to produce the mature natural product is then carried out in vitro with either a commercial protease or a protease that fulfills this task in the producing organism. This review covers the advances in characterizing these latter cognate proteases from bacterial RiPPs and their utility as sequencedependent proteases. The strategies employed for leader peptide removal have been shown to be remarkably diverse. They include one-step removal by a single protease, two-step removal by two dedicated proteases, and endoproteinase activity followed by aminopeptidase activity by the same protease. Similarly, the localization of the proteolytic step varies from cytoplasmic cleavage to leader peptide removal during secretion to extracellular leader peptide removal. Finally, substrate recognition ranges from highly sequence specific with respect to the leader and/or modified core peptide to nonsequence specific mechanisms.

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Section: Metalloproteasesmentioning

confidence: 60%

Section: ■ Metalloproteasesmentioning

confidence: 99%

Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis

Eslami,

van der Donk

2023

ACS Bio Med Chem Au

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“…There were parallel de novo mutations under elevated O3, linked to genes such as sulfotransferase family, peroxiredoxin activity, and carboxymuconolactone decarboxylase family protein, known for an antioxidative response in the host (Mougous et al, 2002;Chen et al, 2015;Kamariah et al, 2018). We found one unique mutation in the pathogen population from a resistant cultivar under elevated O3 by the end-season, which was related to an intergenic region of genes known as TldD protein, identified under different stresses (Vobruba et al, 2022). In addition, possible deleterious sites were identified based on their appearance in mid-season but lost by the end-season.…”

Section: Genetic Differentiation Observed Across Cultivars and O3 Con...mentioning

confidence: 79%

Within-host adaptation of a foliar pathogen,Xanthomonas, on pepper in presence of quantitative resistance and ozone stress

Kaur,

Russell,

Liu

et al. 2024

Preprint

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SummaryThe evolving threat of new pathogen variants in the face of global environmental changes poses a risk to the plant health and can impact the efficacy of resistance-based disease management.Here, we studied short-term eco-evolutionary response of the pathogen,Xanthomonas perforans, on quantitative resistant and susceptible pepper during a single growing season in open-top chambers under the influence of elevated Ozone (O3).We observed increased disease severity, accompanied by higher variation on resistant cultivar under elevated O3, with no apparent change on the susceptible cultivar. This altered resistance response under elevated O3 is linked to altered eco-evolutionary dynamics of pathogen. While a single pathogen genotype remained prevalent on susceptible cultivar, resistant cultivar supported heterogenous pathogen population, with the evidence of short- term evolutionary modifications seeded byde novoparallel mutations. Altered O3 levels led to strain turnover on resistant cultivar with higher within-host polymorphism containing higher proportion of randomde novomutations lacking parallelism.Population heterogeneity is a mechanism of pathogen adaptation in response to the stressors. While parallel mutations in response to quantitative resistance may provide clues to predicting long-term pathogen evolution, high proportion of transient mutations suggest less predictable pathogen evolution under climatic alterations.

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“…The extreme difficulties of managing Xf infections have led to the search for new bactericides able to treat the disease with an eco-friendly approach without compromising the contrasting efficiencies. Many active compounds including toxins, phenolic acids, antibiotics, and AMPs have been reported to be effective against numerous Xf subspecies with minimal bacteriostatic/bactericide concentrations [ 31 , 32 , 33 ]. Moreover, some of these AMPs have been successfully expressed in grapevines to control Xf in greenhouses [ 34 , 35 , 36 ].…”

Section: Discussionmentioning

confidence: 99%

Exploring Active Peptides with Antimicrobial Activity In Planta against Xylella fastidiosa

Handi

Sabri

Valentini

et al. 2022

Biology

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Xylella fastidiosa (Xf) is a xylem-limited quarantine plant bacterium and one of the most harmful agricultural pathogens across the world. Despite significant research efforts, neither a direct treatment nor an efficient strategy has yet been developed for combatting Xylella-associated diseases. Antimicrobial peptides (AMPs) have been gaining interest as a promising sustainable tool to control pathogens due to their unique mechanism of action, broad spectrum of activity, and low environmental impact. In this study, we disclose the bioactivity of nine AMPs reported in the literature to be efficient against human and plant pathogen bacteria, i.e., Escherichia coli, Staphylococcus aureus, and Pseudomonas aeruginosa, against Xf, through in vitro and in vivo experiments. Based on viable-quantitative PCR (v-qPCR), fluorescence microscopy (FM), optical density (OD), and transmission electron microscopy (TEM) assays, peptides Ascaphin-8 (GF19), DASamP1 (FF13), and DASamP2 (IL14) demonstrated the highest bactericidal and antibiofilm activities and were more efficient than the peptide PB178 (KL29), reported as one of the most potent AMPs against Xf at present. Furthermore, these AMPs showed low to no toxicity when tested on eukaryotic cells. In in planta tests, no Xf disease symptoms were noticed in Nicotiana tabacum plants treated with the AMPs 40 days post inoculation. This study highlighted the high antagonistic activity of newly tested AMP candidates against Xf, which could lead to the development of promising eco-friendly management of Xf-related diseases.

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TldD/TldE peptidases and N-deacetylases: A structurally unique yet ubiquitous protein family in the microbial metabolism

Cited by 4 publications

References 71 publications

Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis

Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis

Within-host adaptation of a foliar pathogen,Xanthomonas, on pepper in presence of quantitative resistance and ozone stress

Exploring Active Peptides with Antimicrobial Activity In Planta against Xylella fastidiosa

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