Cloning and characterization of two endoxylanases from the cereal phytopathogen Fusarium graminearum and their inhibition profile against endoxylanase inhibitors from wheat

Beliën, Tim; Campenhout, Steven Van; Acker, Maarten Van; Volckaert, Guido

doi:10.1016/j.bbrc.2004.12.036

Cited by 60 publications

(34 citation statements)

References 27 publications

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“…TAXI can only inhibit GH11 xylanases, which are b-jelly roll proteins that fold like a hand with the catalytic glutamine residues in the 'palm', covered by a 'thumb' [10]. TAXI-I Extracellular enzymeinhibitor interactions Misas-Villamil and van der Hoorn 381 [42 ,48 ] inhibits XylA and XylB, two GH11 xylanases from F. graminearum [11 ]. XynBc1, a GH11 xylanase cloned from Botrytis cinerea, was inhibited by TAXI-I but not by TAXI-II, suggesting that these inhibitors can be specific and have perhaps coevolved with their targets [12 ].…”

Section: Wheat Inhibitor Taxi Targets Pathogen Gh11 Xylanasesmentioning

confidence: 99%

“…GH11 xylanase inhibition is mediated by a loop that sticks in the active site, where an arginine residue directly contacts the catalytic residues of the xylanase ( Figure 2c) [10]. XIP-I is an efficient inhibitor of Botrytis XynBc1 GH11 xylanase [12 ] but it cannot inhibit XylA and XylB GH11 xylanases of F. graminearum [11 ]. Mutagenesis revealed that the absence of inhibition was because of amino acid adaptations in the 'thumb' structural region [21 ].…”

Section: Wheat Inhibitor Xip-i Targets Fungal Gh11 and Gh10 Xylanasesmentioning

confidence: 99%

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Enzyme–inhibitor interactions at the plant–pathogen interface

Misas-Villamil

Hoorn

2008

Current Opinion in Plant Biology

120

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The plant apoplast during plant-pathogen interactions is an ancient battleground that holds an intriguing range of attacking enzymes and counteracting inhibitors. Examples are pathogen xylanases and polygalacturonases that are inhibited by plant proteins like TAXI, XIP, and PGIP; and plant glucanases and proteases, which are targeted by pathogen proteins such as GIP1, EPI1, EPIC2B, and AVR2. These seven well-characterized inhibitors have different modes of action and many probably evolved from inactive enzymes themselves. Detailed studies of the structures, sequence variation, and mutated proteins uncovered molecular struggles between these enzymes and their inhibitors, resulting in positive selection for variant residues at the contact surface, where single residues determine the outcome of the interaction. Introduction Extracellular plant-pathogen interactions probably existed long before the evolution of pathogen effector translocation systems and plant resistance (R) genes. The molecular basis of these interactions is mostly undiscovered but some have been investigated in detail and reveal intriguing mechanisms. Here we will highlight major recent findings of extracellular enzyme-inhibitor interactions at the plant-pathogen interface.Although extracellular plant-pathogen interactions are complex, they can be simplified by assuming that they evolved in several stages (Figure 1). First, micro-organisms became pathogens by attacking plants using cell-wall-degrading enzymes and other hydrolases ( Figure 1A). In response to this attack, plants secrete inhibitors that suppress these hydrolases ( Figure 1B). Initially, these inhibitors were probably constitutively produced, but upon evolution of pathogen recognition systems the production and secretion of these proteins became inducible, becoming part of the arsenal of pathogenesis-related (PR) proteins. Besides suppression of pathogen attack, counter attack mechanisms also evolved in plants through the induced secretion of hydrolytic enzymes ( Figure 1C). Examples are the well-studied PR proteins including endo-b-1,3-glucanases (PR-2), chitinases (PR-3), and proteases (PR-7) [1 ]. Pathogens, in turn, responded to this counter attack by producing inhibitors that suppress these enzymes ( Figure 1D). The fifth and latest step was a sophisticated refinement of the pathogen recognition system by the evolution of R genes that recognize the manipulation of plant targets by pathogens, inducing a severe defense response that includes cell death ( Figure 1E). Aspects of this simplified model are consistent with the 'zigzag' model for the plant immune system, which explains the suppression of basal defense responses by pathogen effector proteins, followed by the evolution of efficient effector recognition by R proteins [2].Antagonistic interactions between organisms at the molecular level result in enzymes that evade inhibition, and inhibitors that adapt to these new enzymes. These 'molecular struggles' result in positive selection for variation of residues at the interactio...

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Section: Wheat Inhibitor Taxi Targets Pathogen Gh11 Xylanasesmentioning

confidence: 99%

Section: Wheat Inhibitor Xip-i Targets Fungal Gh11 and Gh10 Xylanasesmentioning

confidence: 99%

Enzyme–inhibitor interactions at the plant–pathogen interface

Misas-Villamil

Hoorn

2008

Current Opinion in Plant Biology

120

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“…These glycosylated proteins have a single elliptical (ß/a)8-scaffold, the top of which is decorated by loops arranged to form a long depression running along one face of the molecule [12]. XIP can inhibit fungal xylanases from both GH10 and GH11 in a competitive manner [13], with some exceptions [14,15]. In addition, the three dimensional structures of XIP in complex with a GH11 xylanase from Penicillium funiculosum (XPF), on the one hand, and with a GH10 xylanase from Aspergillus nidulans, on the other hand, show a 1:1 complexation ratio for both enzymes and two distinct binding sites.…”

Section: Introductionmentioning

confidence: 99%

“…TAXI and/or XIP inhibit GH 11 xylanases of the phytopathogens Fusarium graminearum and Botrytis cinerea [15,18], and both TAXI and XIP genes are induced by pathogens and wounding [19,20]. In addition, a regulatory role in plant development is disaffirmed by their distinct specificity towards xylanases of microbial origin and their lack of activity against endogenous xylanases [14,21].…”

Section: Introductionmentioning

confidence: 99%

Biochemical and structural characterization of TLXI, the Triticum aestivum L. thaumatin-like xylanase inhibitor

Fierens

Gebruers

Voet

et al. 2009

Journal of Enzyme Inhibition and Medicinal Chemistry

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Thaumatin-like xylanase inhibitors (TLXI) are recently discovered wheat proteins. They belong to the family of the thaumatin-like proteins and inhibit glycoside hydrolase family 11 endoxylanases commonly used in different cereal based (bio)technological processes. We here report on the biochemical characterisation of TLXI. Its inhibition activity is temperature-and pH-dependent and shows a maximum at approximately 408C and pH 5.0. The TLXI structure model, generated with the crystal structure of thaumatin as template, shows the occurrence of five disulfide bridges and three b-sheets. Much as in the structures of other short-chain thaumatin-like proteins, no a-helix is present. The circular dichroism spectrum of TLXI confirms the absence of a-helices and the presence of antiparallel b-sheets. All ten cysteine residues in TLXI are involved in disulfide bridges. TLXI is stable for at least 120 min between pH 1-12 and for at least 2 hours at 1008C, making it much more stable than the other two xylanase inhibitors from wheat, i.e. Triticum aestivum xylanase inhibitor (TAXI) and xylanase inhibitor protein (XIP). This high stability can probably be ascribed to the high number of disulfide bridges, much as seen for other thaumatin-like proteins.

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“…Entretanto, algumas enzimas possuem valores bem distintos, como as xilanases produzidas VAN ACKER, 2005;DUTTA et al, 2007). Ademais, essas xilanases tendem a ser estáveis em uma extensa faixa de pH (2,0-9,0).…”

Section: Propriedades Bioquímicasunclassified

Estudo das propriedades físico-químicas e funcionais de uma endo-1,4-B-xilanase de Aspergillus tamarii Kita e a sua aplicação na produção de xilooligossacarídeos

Heinen¹

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Cloning and characterization of two endoxylanases from the cereal phytopathogen Fusarium graminearum and their inhibition profile against endoxylanase inhibitors from wheat

Cited by 60 publications

References 27 publications

Enzyme–inhibitor interactions at the plant–pathogen interface

Enzyme–inhibitor interactions at the plant–pathogen interface

Biochemical and structural characterization of TLXI, the Triticum aestivum L. thaumatin-like xylanase inhibitor

Estudo das propriedades físico-químicas e funcionais de uma endo-1,4-B-xilanase de Aspergillus tamarii Kita e a sua aplicação na produção de xilooligossacarídeos

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