Atypical features of a Ure2p glutathione transferase from <i>Phanerochaete chrysosporium</i>

Thuillier, Anne; Roret, Thomas; Favier, F.; Gelhaye, Éric; Jacquot, Jean‐Pierre; Didierjean, Claude; Morel‐Rouhier, Mélanie

doi:10.1016/j.febslet.2013.05.031

Cited by 22 publications

(25 citation statements)

References 22 publications

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“…The Ure2p class was split into two subclasses (Ure2pA and Ure2pB). AbUre2pB1 clustered within the Ure2pB subclass, however it exhibited a glutathionylation activity like the yeast isoform, which belongs to the Ure2pA subclass, rather than the deglutathionylation activity previously measured for Ure2pB in P. chrysposporium and E. coli [33, 34]. …”

Section: Resultsmentioning

confidence: 99%

“…However, contrary to the ∆ AbGTT1.2 mutant, the ∆ AbUre2pB1 mutant showed increased susceptibility to ITC and decreased aggressiveness compared to the wild-type strain. The first structural and biochemical characterization of a fungal Ure2pB GST (PcUre2pB1 from Phanerochaete chrysosporium ) was recently published [33]. Unlike PcUre2pB1, AbUre2pB1 did not depict any activity in deglutathionylation tests with β-ME-SG.…”

Section: Discussionmentioning

confidence: 99%

“…Based on our results, it is therefore difficult to come up with any convincing explanation concerning the role of this enzyme in protection against ITCs and in pathogenesis, but they raise interesting questions concerning the evolution of these enzymes. It should be noted that, besides small molecules, PcUre2pB1 was also shown to be involved in glutathionylation/deglutathionylation of proteins, particularly to interact with a GST from the omega class of P. chrysosporium, PcGSTO3 [33]. As AbGSTO1 and AbUre2pB1 have comparable expression patterns and mutants deficient for these two GSTs have similar phenotypes, it would be interesting to check whether these two proteins could also interact and cooperate to protect the fungal cell against ITC toxicity.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of glutathione transferases involved in the pathogenicity of Alternaria brassicicola

et al. 2015

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BackgroundGlutathione transferases (GSTs) represent an extended family of multifunctional proteins involved in detoxification processes and tolerance to oxidative stress. We thus anticipated that some GSTs could play an essential role in the protection of fungal necrotrophs against plant-derived toxic metabolites and reactive oxygen species that accumulate at the host-pathogen interface during infection.ResultsMining the genome of the necrotrophic Brassica pathogen Alternaria brassicicola for glutathione transferase revealed 23 sequences, 17 of which could be clustered into the main classes previously defined for fungal GSTs and six were ‘orphans’. Five isothiocyanate-inducible GSTs from five different classes were more thoroughly investigated. Analysis of their catalytic properties revealed that two GSTs, belonging to the GSTFuA and GTT1 classes, exhibited GSH transferase activity with isothiocyanates (ITC) and peroxidase activity with cumene hydroperoxide, respectively. Mutant deficient for these two GSTs were however neither more susceptible to ITC nor less aggressive than the wild-type parental strain. By contrast mutants deficient for two other GSTs, belonging to the Ure2pB and GSTO classes, were distinguished by their hyper-susceptibility to ITC and low aggressiveness against Brassica oleracea. In particular AbGSTO1 could participate in cell tolerance to ITC due to its glutathione-dependent thioltransferase activity. The fifth ITC-inducible GST belonged to the MAPEG class and although it was not possible to produce the soluble active form of this protein in a bacterial expression system, the corresponding deficient mutant failed to develop normal symptoms on host plant tissues.ConclusionsAmong the five ITC-inducible GSTs analyzed in this study, three were found essential for full aggressiveness of A. brassicicola on host plant. This, to our knowledge is the first evidence that GSTs might be essential virulence factors for fungal necrotrophs.Electronic supplementary materialThe online version of this article (doi:10.1186/s12866-015-0462-0) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Characterization of glutathione transferases involved in the pathogenicity of Alternaria brassicicola

et al. 2015

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“…It has been subdivided into ever-increasing numbers of classes based on a variety of criteria, including amino acid/nucleotide sequences, and immunological, kinetic, and structural properties. Considering their amino acid sequence identities and several other aspects, nine classes of cytosolic GSTs have been described to date in fungi, including GTT1, GTT2, Ure2p, MAK16, EFB1, etherase-like (recently renamed GSTFuA) [ 18 , 19 ], phi [ 20 ], omega, and glutathionyl hydroquinone reductase (GHR) [ 12 , 21 ] in addition to a number of uncharacterized classes. However, due to their structural and immunological differences compared with other organisms, a uniform classification of fungal GSTs has not been reached a consensus [ 12 , 17 , 20 , 21 ].…”

Section: Introductionmentioning

confidence: 99%

Identification of Glutathione S-Transferase (GST) Genes from a Dark Septate Endophytic Fungus (Exophiala pisciphila) and Their Expression Patterns under Varied Metals Stress

et al. 2015

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Glutathione S-transferases (GSTs) compose a family of multifunctional enzymes that play important roles in the detoxification of xenobiotics and the oxidative stress response. In the present study, twenty four GST genes from the transcriptome of a metal-tolerant dark septate endophyte (DSE), Exophiala pisciphila, were identified based on sequence homology, and their responses to various heavy metal exposures were also analyzed. Phylogenetic analysis showed that the 24 GST genes from E. pisciphila (EpGSTs) were divided into eight distinct classes, including seven cytosolic classes and one mitochondrial metaxin 1-like class. Moreover, the variable expression patterns of these EpGSTs were observed under different heavy metal stresses at their effective concentrations for inhibiting growth by 50% (EC50). Lead (Pb) exposure caused the up-regulation of all EpGSTs, while cadmium (Cd), copper (Cu) and zinc (Zn) treatments led to the significant up-regulation of most of the EpGSTs (p < 0.05 to p < 0.001). Furthermore, although heavy metal-specific differences in performance were observed under various heavy metals in Escherichia coli BL21 (DE3) transformed with EpGSTN-31, the over-expression of this gene was able to enhance the heavy metal tolerance of the host cells. These results indicate that E. Pisciphila harbored a diverse of GST genes and the up-regulated EpGSTs are closely related to the heavy metal tolerance of E. pisciphila. The study represents the first investigation of the GST family in E. pisciphila and provides a primary interpretation of heavy metal detoxification for E. pisciphila.

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“…In this specific case, we could speculate that the cysteine found after the threonine position acts as the catalytic residue. Although this will have to be confirmed experimentally, it is interesting to note that poplar GSTF3 and F7 and their close orthologs also have a cysteine at this position, and that fungal Ure2p-like enzymes have an asparagine that was recently assumed to be important for catalysis (Thuillier et al, 2013 ). Overall, this suggests that all residues forming the active site signature and present around the N-terminal end of α1 could substitute to each other.…”

Section: Discussionmentioning

confidence: 98%

The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1

et al. 2014

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Glutathione transferases (GSTs) constitute a superfamily of enzymes with essential roles in cellular detoxification and secondary metabolism in plants as in other organisms. Several plant GSTs, including those of the Phi class (GSTFs), require a conserved catalytic serine residue to perform glutathione (GSH)-conjugation reactions. Genomic analyses revealed that terrestrial plants have around ten GSTFs, eight in the Populus trichocarpa genome, but their physiological functions and substrates are mostly unknown. Transcript expression analyses showed a predominant expression of all genes both in reproductive (female flowers, fruits, floral buds) and vegetative organs (leaves, petioles). Here, we show that the recombinant poplar GSTF1 (PttGSTF1) possesses peroxidase activity toward cumene hydroperoxide and GSH-conjugation activity toward model substrates such as 2,4-dinitrochlorobenzene, benzyl and phenetyl isothiocyanate, 4-nitrophenyl butyrate and 4-hydroxy-2-nonenal but interestingly not on previously identified GSTF-class substrates. In accordance with analytical gel filtration data, crystal structure of PttGSTF1 showed a canonical dimeric organization with bound GSH or 2-(N-morpholino)ethanesulfonic acid molecules. The structure of these protein-substrate complexes allowed delineating the residues contributing to both the G and H sites that form the active site cavity. In sum, the presence of GSTF1 transcripts and proteins in most poplar organs especially those rich in secondary metabolites such as flowers and fruits, together with its GSH-conjugation activity and its documented stress-responsive expression suggest that its function is associated with the catalytic transformation of metabolites and/or peroxide removal rather than with ligandin properties as previously reported for other GSTFs.

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Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium

Cited by 22 publications

References 22 publications

Characterization of glutathione transferases involved in the pathogenicity of Alternaria brassicicola

Characterization of glutathione transferases involved in the pathogenicity of Alternaria brassicicola

Identification of Glutathione S-Transferase (GST) Genes from a Dark Septate Endophytic Fungus (Exophiala pisciphila) and Their Expression Patterns under Varied Metals Stress

The poplar Phi class glutathione transferase: expression, activity and structure of GSTF1

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