All Russian Institute for Plant Protection VIZR

Pushkin, Russia

All Russian Institute for Plant Protection VIZR

Pushkin, Russia
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Konarev A.V.,All Russian Institute for Plant Protection VIZR | Beaudoin F.,Rothamsted Research | Marsh J.,Rothamsted Research | Vilkova N.A.,All Russian Institute for Plant Protection VIZR | And 5 more authors.
Journal of Agricultural and Food Chemistry | Year: 2011

Glutenin hydrolyzing proteinases (GHPs) have been purified, by affinity chromatography, from wheat seeds damaged by the Sunn bug Eurygaster integriceps (Hemiptera, Scutelleridae). A 28 kDa protein was partially sequenced by mass spectrometry and Edman degradation which showed homology to serine proteases from various insects. Three full length clones were obtained from cDNA isolated from Sunn bug salivary glands using degenerate PCR based on the sequences obtained. The cleavage site of the protease was determined using recombinant and synthetic peptides and shown to be between the consensus hexapeptide and nonapeptide repeat motifs present in the high molecular weight subunits of wheat glutenin (PGQGQQ^GYYPTSLQQ). Homology models were generated for the three proteinases identified in this study using the high resolution X-ray structure of a crayfish (Pontastacus leptodactylus) trypsin complexed with a peptide inhibitor as template (PDB accession 2F91). The novel specificity of this protease may find applications in both fundamental and applied studies. © 2011 American Chemical Society.


Gultyaeva E.,All Russian Institute for Plant Protection VIZR | Dmitriev A.,All Russian Institute for Plant Protection VIZR | Kosman E.,Tel Aviv University
Canadian Journal of Plant Pathology | Year: 2012

Four hundred and seventeen single-uredinial isolates of Puccinia triticina collected from wheat in seven regions of Russia in 2007 were tested for virulence with 24 near-isogenic wheat differential lines and molecular variation with six RAPD and one UP-PCR DNA markers. Seventy-nine virulence phenotypes and 71 molecular genotypes were identified. The P. triticina isolates varied for virulence on resistance genes Lr1, Lr2a, Lr2b, Lr2, Lr3a, Lr3bg, Lr3ka, Lr14a, Lr14b, Lr15, Lr16, Lr17, Lr18, Lr19, Lr20, Lr21, Lr24, Lr26, Lr28 and LrB. All isolates were virulent on Lr10, Lr11 and Lr30, and avirulent on Lr9. THTTTJ was the predominant phenotype in all regions with frequency ranging from 25 to 63%. Diversity analysis of the regional collections demonstrated inconsistency of results obtained with virulence and molecular markers. According to the virulence data, the North Caucasian and Central collections of P. triticina were the most distant from all the other regional populations. The most similar were collections from West Siberian and Ural regions, which may be a result of growing genetically similar wheat cultivars. According to the molecular marker data, the Central, Central Black Earth, and Ural populations clustered distinctly from the North Western, North Caucasian, and West Siberian collections. © 2012 The Canadian Phytopathological Society.


PubMed | All Russian Institute for Plant Protection VIZR
Type: Journal Article | Journal: Journal of agricultural and food chemistry | Year: 2011

Glutenin hydrolyzing proteinases (GHPs) have been purified, by affinity chromatography, from wheat seeds damaged by the Sunn bug Eurygaster integriceps (Hemiptera, Scutelleridae). A 28 kDa protein was partially sequenced by mass spectrometry and Edman degradation which showed homology to serine proteases from various insects. Three full length clones were obtained from cDNA isolated from Sunn bug salivary glands using degenerate PCR based on the sequences obtained. The cleavage site of the protease was determined using recombinant and synthetic peptides and shown to be between the consensus hexapeptide and nonapeptide repeat motifs present in the high molecular weight subunits of wheat glutenin (PGQGQQGYYPTSLQQ). Homology models were generated for the three proteinases identified in this study using the high resolution X-ray structure of a crayfish (Pontastacus leptodactylus) trypsin complexed with a peptide inhibitor as template (PDB accession 2F91). The novel specificity of this protease may find applications in both fundamental and applied studies.

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