Molecular characterization of gene sequences coding for protein disulfide isomerase (PDI) in durum wheat (Triticum turgidum ssp. durum )

Ciaffi, M.; Paolacci, Anna Rita; Dominici, Luca; Tanzarella, O. A.; Porceddu, E.

doi:10.1016/s0378-1119(01)00348-1

Cited by 32 publications

(28 citation statements)

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“…In addition, genes like the PDI and COP genes were also induced after BTH and fenpropimorph treatments. Their expression in wheat has been described during plant development (Ciaffi et al, 2001) but not after chemical treatment. These results might indicate that BTH and fenpropimorph induce the secretory and cell surface protein biosynthesis machinery.…”

Section: Discussionmentioning

confidence: 99%

“…belonging to other functional classes were also upregulated. Two protein disulfide isomerase genes and one coatomer protein (COP) subunit gene showed an induction of RNA synthesis after 24 h, suggesting an increased biosynthesis of secreted or cell surface proteins (Harter, 1995;Ciaffi et al, 2001). Genes encoding the putative proteins flavanone-3-hydroxylase and caffeoyl CoA O-methyltransferase, involved in flavonoid biosynthesis, showed an activation of transcription only after one week.…”

Section: Effect Of the Bth Treatmentmentioning

confidence: 99%

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Specific patterns of changes in wheat gene expression after treatment with three antifungal compounds

et al. 2005

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The two fungicides azoxystrobin and fenpropimorph are used against powdery mildew and rust diseases in wheat (Triticum aestivumL). Azoxystrobin, a strobilurin, inhibits fungal mitochondrial respiration and fenpropimorph, a morpholin, represses biosynthesis of ergosterol, the major sterol of fungal membranes. Although the fungitoxic activity of these compounds is well understood, their effects on plant metabolism remain unclear. In contrast to the fungicides which directly affect pathogen metabolism, benzo(1,2,3) thiadiazole-7-carbothioic acid S-methylester (BTH) induces resistance against wheat pathogens by the activation of systemic acquired resistance in the host plant. In this study, we monitored gene expression in spring wheat after treatment with each of these agrochemicals in a greenhouse trial using a microarray containing 600 barley cDNA clones. Defence-related genes were strongly induced after treatment with BTH, confirming the activation of a similar set of genes as in dicot plants following salicylic acid treatment. A similar gene expression pattern was observed after treatment with fenpropimorph and some defence-related genes were induced by azoxystrobin, demonstrating that these fungicides also activate a defence reaction. However, less intense responses were triggered than with BTH. The same experiments performed under field conditions gave dramatically different results. No gene showed differential expression after treatment and defence genes were already expressed at a high level before application of the agrochemicals. These differences in the expression patterns between the two environments demonstrate the importance of plant growth conditions for testing the impact of agrochemicals on plant metabolism.

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Section: Discussionmentioning

confidence: 99%

Section: Effect Of the Bth Treatmentmentioning

confidence: 99%

Specific patterns of changes in wheat gene expression after treatment with three antifungal compounds

et al. 2005

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“…This is mostly achieved with the help of a folding catalyst, for example protein disulfide isomerase, which catalyzes the rearrangements that lead to native disulfides and native tertiary structure (53). Disulfide isomerase proteins have been found previously in numerous other plant organisms, such as soybean (54), wheat (55,56), maize (57), and rice (58). It is therefore highly probable that Amaranthus crop plants have a gene for a disulfide isomerase.…”

Section: Discussionmentioning

confidence: 99%

Oxidative Folding of Amaranthus α-Amylase Inhibitor

Cemazar

Zahariev

Pongor

et al. 2004

Journal of Biological Chemistry

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Oxidative folding is the fusion of native disulfide bond formation with conformational folding. This complex process is guided by two types of interactions: first, covalent interactions between cysteine residues, which transform into native disulfide bridges, and second, non-covalent interactions giving rise to secondary and tertiary protein structure. The aim of this work is to understand both types of interactions in the oxidative folding of Amaranthus ␣-amylase inhibitor (AAI) by providing information both at the level of individual disulfide species and at the level of amino acid residue conformation. The cystine-knot disulfides of AAI protein are stabilized in an interdependent manner, and the oxidative folding is characterized by a high heterogeneity of one-, two-, and three-disulfide intermediates. The formation of the most abundant species, the main folding intermediate, is favored over other species even in the absence of non-covalent sequential preferences. Time-resolved NMR and photochemically induced dynamic nuclear polarization spectroscopies were used to follow the oxidative folding at the level of amino acid residue conformation. Because this is the first time that a complete oxidative folding process has been monitored with these two techniques, their results were compared with those obtained at the level of an individual disulfide species. The techniques proved to be valuable for the study of conformational developments and aromatic accessibility changes along oxidative folding pathways. A detailed picture of the oxidative folding of AAI provides a model study that combines different biochemical and biophysical techniques for a fuller understanding of a complex process.Cracking the code for folding a string of amino acid residues into a biologically active three-dimensional structure is still a major challenge of both chemical and biological interest. The information that determines the folding of a protein is contained solely in its amino acid residues (1). In proteins that contain cysteine residues the formation of disulfide bonds is an additional degree of freedom in the folding process. In these proteins a fusion between the recovery of the native tertiary structure (conformational folding) and the regeneration of native disulfide bonds is coupled in the oxidative folding process (2).Disulfide formation is important for in vivo folding of a considerable number of eukaryotic proteins and is a key posttranslational modification for the stabilization of folded structures. The study of oxidative folding in vitro can provide a detailed structural description in terms of the disulfide intermediate species present along the pathway of the complex folding process. A thorough account of an oxidative folding reaction should combine a study of the formation of covalently stable intermediate species and their disulfide bond connectivity and an analysis of the conformational assembly of these species. An established method for elucidation of the exact role that disulfides play in the process of achieving...

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“…It has been cloned and sequenced in many plant species, such as alfalfa [17], barley [18], maize [19], castor bean [20], soyabean [21][22][23][24], common and durum wheat [25,26]. A detailed knowledge of the complexity and diversity of the genes encoding PDI and PDI-like proteins in Arabidopsis thaliana, wheat and other plant species was described by [27,28].…”

Section: Introductionmentioning

confidence: 99%

“…Chinese Spring (CS) (Ciaffi et al, 2006) showed that the PDI transcripts, although constitutively present at a low level in all the analyzed tissues, are equally abundant in the developing caryopses but are differentially expressed in spikelets, roots and leaves [25,31]. The PDI-4A transcription was higher in spikelets, that of PDI-4B were higher in roots while the PDI-4 D transcripts were more abundant in leaves.…”

Section: Introductionmentioning

confidence: 99%

Evolutionary Relationship of Wheat Protein Disulphide Isomerase (PDI) Gene Promoter Sequence Based on Phylogenetic Analysis

Dhanapal¹

2012

AJPS

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Protein disulphide isomerase (PDI) is an oxidoreductase enzyme abundant in the endoplasmic reticulum (ER). In plants, PDIs have been shown to assist the folding and deposition of seed storage proteins during the biogenesis of protein bodies in the endosperm. Cloning and characterization of the complete set of genes encoding PDI and PDI like proteins in bread wheat (Triticum aestivum cv. Chinese Spring) and the comparison of their sequence, structure and expression with homologous genes from other plant species were reported in our previous publications. Promoter sequences of three homoeologous genes encoding typical PDI, located on chromosome group 4 of bread wheat, and PDI promoter sequence analysis of Triticum urartu, Aegilops speltoides and Aegilops tauschii had also been reported previously. In this study, we report the isolation and sequencing of a ~700 bp region, comprising ~600 bp of the putative promoter region and 88 bp of the first exon of the typical PDI gene, in five accessions each from Triticum urartu (AA), Aegilops speltoides (BB) and Aegilops tauschii (DD). Sequence analysis indicated large variation among sequences belonging to the different genomes, while close similarity was found within each species and with the corresponding homoeologous PDI sequences of Triticum aestivum cv. CS (AABBDD) resulting in an overall high conservation of the sequence conferring endosperm-specific expression.

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Molecular characterization of gene sequences coding for protein disulfide isomerase (PDI) in durum wheat (Triticum turgidum ssp. durum )

Cited by 32 publications

References 31 publications

Specific patterns of changes in wheat gene expression after treatment with three antifungal compounds

Specific patterns of changes in wheat gene expression after treatment with three antifungal compounds

Oxidative Folding of Amaranthus α-Amylase Inhibitor

Evolutionary Relationship of Wheat Protein Disulphide Isomerase (PDI) Gene Promoter Sequence Based on Phylogenetic Analysis

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