3-to-1: unraveling structural transitions in ureases

Ligabue-Braun, Rodrigo; Andreis, Fábio Carrer; Verli, Hugo; Carlini, Célia R.

doi:10.1007/s00114-013-1045-2

Cited by 31 publications

(16 citation statements)

References 65 publications

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“…Urease and Msr can be found in plants, fungi, archaea, and bacteria (59,60). Throughout the three domains of life, urease is increasingly seen as a "moonlighting protein" with a variety of noncatalytic roles, including fungicidal, insecticidal, and proinflammatory effects (61).…”

Section: Discussionmentioning

confidence: 99%

Noncatalytic Antioxidant Role for Helicobacter pylori Urease

et al. 2018

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The well-studied catalytic role of urease, the Ni-dependent conversion of urea into carbon dioxide and ammonia, has been shown to protect against the low pH environment of the stomach lumen. We hypothesized that the abundantly expressed urease protein can play another, non-catalytic role in combating oxidative stress via Met-residue mediated quenching of harmful oxidants. Three catalytically inactive urease mutant strains were constructed by single substitutions of Ni binding residues. The mutant versions synthesize normal levels of urease and the altered versions retain all methionine residues. The three site-directed urease mutants were able to better withstand a hypochlorous acid (HOCl) challenge than a Δ deletion strain. The capacity of purified urease to protect whole cells via oxidant quenching was assessed by adding urease enzyme to non-growing HOCl-exposed cells. No wild type cells were recovered with oxidant alone, whereas urease addition significantly aided viability. These results suggest that urease can protect against oxidative damage and that the protective ability is distinct from the well characterized catalytic role. In order to determine the capability of Msr to reduce oxidized Met residues in urease, purified urease was exposed to HOCl and a previously-described Msr peptide repair mixture was added. Of the 25 methionine residues in urease, 11 were subject to both oxidation and to Msr-mediated repair, as identified by MS analysis; therefore the oxidant quenchable Met pool comprising urease can be recycled by the Msr repair system. Non-catalytic urease appears to play an important role in oxidant protection. Chronic infection can lead to gastric ulcers and gastric cancers. The enzyme urease contributes to the survival of the bacterium in the harsh environment of the stomach through increasing the local pH. In addition to combating acid, must survive host-produced reactive oxygen species in order to persist in the gastric mucosa. We describe a cyclic amino acid based antioxidant role of urease, whereby oxidized methionine residues can be recycled by methionine sulfoxide reductase to again quench oxidants. This work expands our understanding of the role of an already-acknowledged pathogen virulence factor and specifically expands our knowledge of survival mechanisms.

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Section: Discussionmentioning

confidence: 99%

Noncatalytic Antioxidant Role for Helicobacter pylori Urease

et al. 2018

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“…Regarding the evolutionary age of ureases in plants, they are generally considered to be as old as plants; themselves nevertheless, a putative horizontal transfer of prokaryotic origin to unicellular algae is suggested 35 . The phylogenetic tree constructed in our work, including seven species of carnivorous plants, is in agreement with the tree encompassing ureases from all domains of life 35 . It is also in agreement with the plant phylogeny, as confirmed by comparison with the Interactive Tree of Life using the PhyloT tool from iTOL 3.0 36 .…”

Section: Discussionmentioning

confidence: 99%

“…Amino acid sequences of plant and fungal ureases were retrieved from the National Center for Biotechnology Information 52 based on a previous urease phylogeny study by Ligabue-Braun and colleagues 35 . These sequences, along with the sequences of ureases from additional carnivorous plants presented here were aligned using MAFTT5 53 and filtered for unreliable positions using Guidance2 54 .…”

Section: Methodsmentioning

confidence: 99%

Coprophagous features in carnivorous Nepenthes plants: a task for ureases

Yilamujiang

Zhu

Ligabue-Braun

et al. 2017

Sci Rep

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Most terrestrial carnivorous plants are specialized on insect prey digestion to obtain additional nutrients. Few species of the genus Nepenthes developed mutualistic relationships with mammals for nitrogen supplementation. Whether dietary changes require certain enzymatic composition to utilize new sources of nutrients has rarely been tested. Here, we investigated the role of urease for Nepenthes hemsleyana that gains nitrogen from the bat Kerivoula hardwickii while it roosts inside the pitchers. We hypothesized that N. hemsleyana is able to use urea from the bats’ excrements. In fact, we demonstrate that 15N-enriched urea provided to Nepenthes pitchers is metabolized and its nitrogen is distributed within the plant. As ureases are necessary to degrade urea, these hydrolytic enzymes should be involved. We proved the presence and enzymatic activity of a urease for Nepenthes plant tissues. The corresponding urease cDNA from N. hemsleyana was isolated and functionally expressed. A comprehensive phylogenetic analysis for eukaryotic ureases, including Nepenthes and five other carnivorous plants’ taxa, identified them as canonical ureases and reflects the plant phylogeny. Hence, this study reveals ureases as an emblematic example for an efficient, low-cost but high adaptive plasticity in plants while developing a further specialized lifestyle from carnivory to coprophagy.

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“…Ureases are enzymes that catalyze the hydrolysis of urea into carbon dioxide and ammonia, being widespread in plants, fungi, and bacteria, but they are not synthesized by animals (Ligabue‐Braun, Andreis, Verli, & Carlini, 2013; Mobley & Hausinger, 1989). The ureases from Canavalia ensiformis have been described as moonlighting proteins, presenting fungi‐ and entomotoxic properties that are not related with their enzymatic functions (Carlini & Ligabue‐Braun, 2016).…”

Section: Introductionmentioning

confidence: 99%

Jaburetox, a urease‐derived peptide: Effects on enzymatic pathways of the cockroach Nauphoeta cinerea

Perin

Noronha

Moyetta

et al. 2020

Arch Insect Biochem Physiol

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Jaburetox is a recombinant peptide derived from one of the Canavalia ensiformis urease isoforms. This peptide induces several toxic effects on insects of different orders, including interference on muscle contractility in cockroaches, modulation of UDP‐N‐acetylglucosamine pyrophosphorylase (UAP) and nitric oxide synthase (NOS) activities in the central nervous system of triatomines, as well as activation of the immune system in Rhodnius prolixus. When injected, the peptide is lethal for R. prolixus and Triatoma infestans. Here, we evaluated Jaburetox toxicity to Nauphoeta cinerea cockroaches, exploring the effects on the central nervous system through the activities of UAP, NOS, acid phosphatases (ACP), and acetylcholinesterase (AChE). The results indicated that N. cinerea is not susceptible to the lethal effect of the peptide. Moreover, both in vivo and in vitro treatments with Jaburetox inhibited NOS activity, without modifying the protein levels. No alterations on ACP activity were observed. In addition, the enzyme activity of UAP only had its activity affected at 18 hr after injection. The peptide increased the AChE activity, suggesting a mechanism involved in overcoming the toxic effects. In conclusion, our findings indicate that Jaburetox affects the nitrinergic signaling as well as the AChE and UAP activities and establishes N. cinerea as a Jaburetox‐resistant model for future comparative studies.

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3-to-1: unraveling structural transitions in ureases

Cited by 31 publications

References 65 publications

Noncatalytic Antioxidant Role for Helicobacter pylori Urease

Noncatalytic Antioxidant Role for Helicobacter pylori Urease

Coprophagous features in carnivorous Nepenthes plants: a task for ureases

Jaburetox, a urease‐derived peptide: Effects on enzymatic pathways of the cockroach Nauphoeta cinerea

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