Crystal Structures of Two Homologous Pathogenesis-related Proteins from Yellow Lupine

Biesiadka, Jacek; Bujacz, G.; Sikorski, M.; Jaskólski, Mariusz

doi:10.1016/s0022-2836(02)00385-6

Cited by 89 publications

(95 citation statements)

References 59 publications

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“…1105/tpc.105.037119 demonstrated to play a role in plant development and during pathogen infection (van Loon and van Strien, 1999). To date, the structures of six plant PR-10 proteins have been reported (Gajhede et al, 1996;Neudecker et al, 2001;Biesiadka et al, 2002;Pasternak et al, 2005;Schirmer et al, 2005). The PR-10 fold consists of a curved b-sheet and a long C-terminal a-helix (a3), which enclose a large cavity within the protein core.…”

Section: Introductionmentioning

confidence: 99%

Crystal Structure of Vigna radiata Cytokinin-Specific Binding Protein in Complex with Zeatin

et al. 2006

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The cytosolic fraction of Vigna radiata contains a 17-kD protein that binds plant hormones from the cytokinin group, such as zeatin. Using recombinant protein and isothermal titration calorimetry as well as fluorescence measurements coupled with ligand displacement, we have reexamined the K d values and show them to range from ;10 ÿ6 M (for 4PU30) to 10 ÿ4 M (for zeatin) for 1:1 stoichiometry complexes. In addition, we have crystallized this cytokinin-specific binding protein (Vr CSBP) in complex with zeatin and refined the structure to 1.2 Å resolution. Structurally, Vr CSBP is similar to plant pathogenesisrelated class 10 (PR-10) proteins, despite low sequence identity (<20%). This unusual fold conservation reinforces the notion that classic PR-10 proteins have evolved to bind small-molecule ligands. The fold consists of an antiparallel b-sheet wrapped around a C-terminal a-helix, with two short a-helices closing a cavity formed within the protein core. In each of the four independent CSBP molecules, there is a zeatin ligand located deep in the cavity with conserved conformation and protein-ligand interactions. In three cases, an additional zeatin molecule is found in variable orientation but with excellent definition in electron density, which plugs the entrance to the binding pocket, sealing the inner molecule from contact with bulk solvent.

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Section: Introductionmentioning

confidence: 99%

Crystal Structure of Vigna radiata Cytokinin-Specific Binding Protein in Complex with Zeatin

et al. 2006

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“…PR proteins, which function in a wide range of processes related to signal transduction and antimicrobial activity (Zubini et al, 2009), have been classified into 17 families based on structural features; of these, the PR-10 protein family is a large group containing more than 100 members (Somssich et al, 1988;Biesiadka et al, 2002;Hashimoto et al, 2004;Xu et al, 2014), which are typically small and localized in the cytosol (Fernandes et al, 2013). PR-10 proteins play multifunctional roles in defense mechanisms against abiotic and biotic stresses, and in developmental regulation via their RNase activity and/ or interaction with ligands (Fernandes et al, 2013;Agarwal and Agarwal, 2014).…”

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confidence: 99%

An Ethylene-Induced Regulatory Module Delays Flower Senescence by Regulating Cytokinin Content

Jia

et al. 2016

Plant Physiol.

103

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ORCID IDs: 0000-0002-6288-7917 (Y.J.); 0000-0002-5972-7963 (C.-Z.J.); 0000-0002-3866-0894 (C.M.); 0000-0002-9285-2539 (J.G.).In many plant species, including rose (Rosa hybrida), flower senescence is promoted by the gaseous hormone ethylene and inhibited by the cytokinin (CTK) class of hormones. However, the molecular mechanisms underlying these antagonistic effects are not well understood. In this study, we characterized the association between a pathogenesis-related PR-10 family gene from rose (RhPR10.1) and the hormonal regulation of flower senescence. Quantitative reverse transcription PCR analysis showed that RhPR10.1 was expressed at high levels during senescence in different floral organs, including petal, sepal, receptacle, stamen, and pistil, and that expression was induced by ethylene treatment. Silencing of RhPR10.1 expression in rose plants by virusinduced gene silencing accelerated flower senescence, which was accompanied by a higher ion leakage rate in the petals, as well as increased expression of the senescence marker gene RhSAG12. CTK content and the expression of three CTK signaling pathway genes were reduced in RhPR10.1-silenced plants, and the accelerated rate of petal senescence that was apparent in the RhPR10.1-silenced plants was restored to normal levels by CTK treatment. Finally, RhHB6, a homeodomain-Leu zipper I transcription factor, was observed to bind to the RhPR10.1 promoter, and silencing of its expression also promoted flower senescence. Our results reveal an ethylene-induced RhHB6-RhPR10.1 regulatory module that functions as a brake of ethylenepromoted senescence through increasing the CTK content.

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“…P-loop, is a phosphatebinding loop found in nucleotide binding proteins [18]. However, PR-10 proteins do not have affinity for ATP and the glycine-rich loop is conformationally different from the P-loop [19][20]. Interestingly, the glycine-rich loop is the most rigid structural element in the PR-10 fold despite being glycine rich.…”

Section: Pr-10 Proteins: An Overviewmentioning

confidence: 99%

“…However, Biesiadka et al [20] reported that despite having a high level (76.8%) of identity and sequence conservation at the RNase-relevant positions in two yellow lupine LlPR-10.1A and LlPR-10.1B proteins, only LlPR-10.1B showed RNase activity. Therefore, it is presumed that RNase activity is found in some PR10 proteins, but this is not a general property of this class of PR proteins.…”

Section: Pr-10 Proteins: An Overviewmentioning

confidence: 99%

“…A large internal Y-shaped hydrophobic cavity, as determined by three-dimensional structure of PR-10 proteins could be liable for transport of a polar ligands such as fatty acids, flavonoids, cytokinins or brassino steroids in the intracellular spaces [62]. The diverse roles predicted for PR-10 proteins in the plant immune system should have consideration of discernable modifications of the structure and shape of this cavity allowing to bind different ligands [20,63].…”

Section: Pr-10 Proteins: An Overviewmentioning

confidence: 99%

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The Pathogenesis Related Class 10 proteins in Plant Defense against Biotic and Abiotic Stresses

Jain¹

2015

APAR

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One of the most represented group of Pathogenesis Related (PR) genes are those of the PR-10 class. PR-10 proteins are members of multi genic family, and they often occur in clusters at specific loci following gene duplication and amplification events. To date, large number of PR-10 genes have been cloned and characterized in different species in response to abiotic and biotic stress. This review is focused on recent studies that have described the role, distribution and structure of PR-10 genes in plant genomes. Recent findings have provided insights into the functional roles of PR-10 proteins as ribonuclease, as cytokinin-specific binding proteins, a mammalian lipid transport and plant abscisic acid (ABA) receptor proteins, or as enzyme, (S)-norco claurine synthase. PR-10 proteins are differentially expressed in the presence of different signaling molecules, biotic stresses such as fungal, viral and bacterial pathogens and a number of abiotic stresses. The possibility to use this knowledge for genetic improvement of plant resistance to pathogens through classical breeding approach or transgenic technology is discussed.

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Crystal Structures of Two Homologous Pathogenesis-related Proteins from Yellow Lupine

Cited by 89 publications

References 59 publications

Crystal Structure of Vigna radiata Cytokinin-Specific Binding Protein in Complex with Zeatin

Crystal Structure of Vigna radiata Cytokinin-Specific Binding Protein in Complex with Zeatin

An Ethylene-Induced Regulatory Module Delays Flower Senescence by Regulating Cytokinin Content

The Pathogenesis Related Class 10 proteins in Plant Defense against Biotic and Abiotic Stresses

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