Structural Basis for Inhibition of Aspergillus niger Xylanase by Triticum aestivum Xylanase Inhibitor-I

Sansen, Stefaan; Ranter, C. J. De; Gebruers, Kurt; Brijs, Kristof; Courtin, Christophe M.; Delcour, Jan A.; Rabijns, A.

doi:10.1074/jbc.m404212200

Cited by 115 publications

(136 citation statements)

References 45 publications

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“…TAXI-I Extracellular enzymeinhibitor interactions Misas-Villamil and van der Hoorn 381 However, these interactions are just the tip of the iceberg, as F. graminearum has over 30 different xylanase genes that are induced during infection [13]. The crystal structure of TAXI has a striking structural homology with pepsin-like aspartic proteases but it lacks the required catalytic triad, suggesting that this inhibitor evolved from a pepsin-like aspartic protease ancestor [14]. The crystal structure of the complex of TAXI-I inhibiting the Aspergillus niger xylanase-I (ANXI) revealed substrate-mimicking contacts in the substrate-docking region of the xylanase [14] (Figure 2a).…”

Section: Wheat Inhibitor Taxi Targets Pathogen Gh11 Xylanasesmentioning

confidence: 99%

“…The crystal structure of TAXI has a striking structural homology with pepsin-like aspartic proteases but it lacks the required catalytic triad, suggesting that this inhibitor evolved from a pepsin-like aspartic protease ancestor [14]. The crystal structure of the complex of TAXI-I inhibiting the Aspergillus niger xylanase-I (ANXI) revealed substrate-mimicking contacts in the substrate-docking region of the xylanase [14] (Figure 2a). The TAXI-GH11 interactions probably hold a wealth of information on molecular struggles, to be revealed by determining positions for diversifying selection and their importance for the interaction.…”

Section: Wheat Inhibitor Taxi Targets Pathogen Gh11 Xylanasesmentioning

confidence: 99%

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Enzyme–inhibitor interactions at the plant–pathogen interface

Misas-Villamil

Hoorn

2008

Current Opinion in Plant Biology

111

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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 Taxi Targets Pathogen Gh11 Xylanasesmentioning

confidence: 99%

Enzyme–inhibitor interactions at the plant–pathogen interface

Misas-Villamil

Hoorn

2008

Current Opinion in Plant Biology

111

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“…These data indicate that although these proteases belong to the A1B subfamily, they are unable to display catalytic activities. An NCBI-BLAST search of these sequences indicated that the two proteins might be xylanase and endoglucanase inhibitor proteins, which are involved in plant defense (38). Taken together, two of the putative aspartic proteases are likely not involved in the degradation of prey proteins in the Venus flytrap.…”

Section: The Composition Of the Digestive Fluid Of The Venus Flytrapmentioning

confidence: 99%

The Protein Composition of the Digestive Fluid from the Venus Flytrap Sheds Light on Prey Digestion Mechanisms

Schulze

Sanggaard

Kreuzer

et al. 2012

Molecular & Cellular Proteomics

107

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The Venus flytrap (Dionaea muscipula) is one of the most well-known carnivorous plants because of its unique ability to capture small animals, usually insects or spiders, through a unique snap-trapping mechanism. The animals are subsequently killed and digested so that the plants can assimilate nutrients, as they grow in mineral-deficient soils. We deep sequenced the cDNA from Dionaea traps to obtain transcript libraries, which were used in the mass spectrometry-based identification of the proteins secreted during digestion. The identified proteins consisted of peroxidases, nucleases, phosphatases, phospholipases, a glucanase, chitinases, and proteolytic enzymes, including four cysteine proteases, two aspartic proteases, and a serine carboxypeptidase. The majority of the most abundant proteins were categorized as pathogenesis-related proteins, suggesting that the plant's digestive system evolved from defense-related processes. This indepth characterization of a highly specialized secreted fluid from a carnivorous plant provides new information about the plant's prey digestion mechanism and the evolutionary processes driving its defense pathways and nutrient acquisition. Molecular & Cellular

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“…TAXI is the other type of xylanase inhibitor isolated from wheat and is specific for GH11 xylanases (35). Both inhibitors show a common inhibition strategy by binding to the active site region (Sansen et al) (38). The different specificities displayed by TAXI-I and XIP-I might be indicative of a distinct role in plant defense depending on the part of the plant that is affected by the infection, the stage in plant development, and the type of pathogens or nature of the isozyme secreted by a pathogen.…”

Section: Determinants Of Specificity Of Xip-imentioning

confidence: 99%

The Dual Nature of the Wheat Xylanase Protein Inhibitor XIP-I

Payan

Leone

Porciero

et al. 2004

Journal of Biological Chemistry

114

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The xylanase inhibitor protein I (XIP-I) from wheatTriticum aestivum is the prototype of a novel class of cereal protein inhibitors that inhibit fungal xylanases belonging to glycoside hydrolase families 10 (GH10) and 11 (GH11). The crystal structures of XIP-I in complex with Aspergillus nidulans (GH10) and Penicillium funiculosum (GH11) xylanases have been solved at 1.7 and 2.5 Å resolution, respectively. The inhibition strategy is novel because XIP-I possesses two independent enzyme-binding sites, allowing binding to two glycoside hydrolases that display a different fold. Inhibition of the GH11 xylanase is mediated by the insertion of an XIP-I ⌸-shaped loop (L␣ 4 ␤ 5 ) into the enzyme active site, whereas residues in the helix ␣7 of XIP-I, pointing into the four central active site subsites, are mainly responsible for the reversible inactivation of GH10 xylanases. The XIP-I strategy for inhibition of xylanases involves substrate-mimetic contacts and interactions occluding the active site. The structural determinants of XIP-I specificity demonstrate that the inhibitor is able to interact with GH10 and GH11 xylanases of both fungal and bacterial origin. The biological role of the xylanase inhibitors is discussed in light of the present structural data.

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Structural Basis for Inhibition of Aspergillus niger Xylanase by Triticum aestivum Xylanase Inhibitor-I

Cited by 115 publications

References 45 publications

Enzyme–inhibitor interactions at the plant–pathogen interface

Enzyme–inhibitor interactions at the plant–pathogen interface

The Protein Composition of the Digestive Fluid from the Venus Flytrap Sheds Light on Prey Digestion Mechanisms

The Dual Nature of the Wheat Xylanase Protein Inhibitor XIP-I

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