Virulence of north american and european races of Puccinia striiformis on north american,world, and european differential wheat cultivars

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Comparison Of Three Methods For Enamel Protein Extraction In Different Developmental Phases Of Rat Lower Incisors

Protein extraction methods [urea, trichloroacetic acid (TCA), and acetic acid] were compared for protein recovery from rat incisor developing enamel in the S phase (intermediate/late secretion), M1 phase (early maturation), M2 phase (intermediate maturation), and M3 phase (final maturation). We compared the protein recoveries with the percentage of enamel matrix dry weight burnt off by incineration. Our results indicate that TCA and urea were equally efficient for the extraction of S-stage proteins (85% and 90% recovery, respectively), while urea was the best for M1-stage proteins (92% recovery), and TCA the best for M2-stage (99% recovery) and M3-stage (60% recovery) proteins. The other methods yielded less than 30% recovery in comparison to incineration for M2 and M3 stages. The fact that urea extraction works well in the S and M1 stages and not thereafter is probably related to the changes in the proteins during enamel development and the amount of mineral that needs to be dissolved. TCA is the single method that effectively recovered proteins from all developmental stages of the rat incisor enamel. © Eur J Oral Sci, 2006.114SUPPL. 1272275Glimcher M, J., Levine, P.T., Studies of the proteins, peptides and free amino acids of mature bovine enamel (1966) Biochem J, 98, pp. 742-753Robinson C, Briggs, H.D., Atkinson, P.J., Weatherell, J.A., Chemical composition of human deciduous enamel (1981) Arch Oral Biol, 26, pp. 1027-1033Simmer J, P., Jc-C, H., Expression, structure, and function of enamel proteinases (2002) Connect Tissue Res, 43, pp. 441-449Smith C, E., Pompura, J.R., Borenstein, S., Fazel, A., Nanci, A., Degradation and loss of matrix proteins from developing enamel (1989) Anat Rec, 224, pp. 292-316Brookes S, J., Robinson, C., Kirkham, J., Bonass, W.A., Biochemistry and molecular biology of amelogenin proteins of developing enamel (1995) Arch Oral Biol, 40, pp. 1-14Glimcher M, J., Brichley-Parsons, D., Levine, P.T., Studies of enamel proteins during maturation (1977) Calcif Tissue Res, 24, pp. 259-270Glimcher M, J., Friberg, U.A., Levine, P.T., The isolation and amino acid composition of the enamel proteins of erupted bovine teeth (1964) Biochem J, 93, pp. 202-210Termine J, D., Belcourt, A.B., Christner, P.J., Conn, K.N., Nylen, M.U., Properties of dissociatively extracted fetal tooth matrix proteins. I. Principal molecular species in developing bovine enamel (1980) J Biol Chem, 255, pp. 9760-9768Belcourt A, B., Fincham, A.G., Termine, J.D., Bovine high molecular weight amelogenin proteins (1983) Calcif Tissue Int, 32, pp. 111-114Fincham A, G., Belcourt, A.B., Lyaruu, D.M., Termine, J.D., Comparative protein biochemistry of developing dental enamel matrix from five mammalian species (1982) Calcif Tissue Int, 34, pp. 182-189Fukae M, Shimizu, M., Studies on the proteins developing bovine enamel (1974) Arch Oral Biol, 19, pp. 381-386Bensadoun A, Weinstein, D., Assay of proteins in the presence of interfering materials (1976) Anal Biochem, 70, pp. 241-150Bradford M, M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254Laemmli U, K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685Rosenberg I, M., (1996) Protein Analysis and Purification: Benchtop Techniques, 1st Edn.Smith C, E., Cellular and chemical events during enamel maturation (1998) Crit Rev Oral Biol Med, 9, pp. 128-161Moradian-Oldak J, Tan, J., Fincham, A.G., Interaction of amelogenin with hydroxyapatite crystals: An adherence effect through amelogenin molecular self association (1998) Biopolymers, 46, pp. 225-238Seyer J, M., Glimcher, M.J., Evidence for the presence of numerous protein components in immature bovine dental enamel (1977) Calcif Tiss Res, 24, pp. 253-25

Development of Sequence Tagged Site and Cleaved Amplified Polymorphic Sequence Markers for Wheat Stripe Rust Resistance Gene Yr5

The Yr5 gene confers resistance to all races of the wheat stripe rust pathogen [Puccinia striiformis Westend. f. sp. tritici Eriks. (P. s. tritici)] identified so far in the USA. Cosegregating resistance gene analog polymorphism (RGAP) markers for Yr5 are available but their use requires skills in polyacrylamide gel electrophoresis and may not be polymorphic across various varieties. To develop better markers to be used in marker-assisted selection for the Yr5 resistance, sequence tagged site (STS) primers were designed on the basis of the sequences of RGAP markers Xwgp-18 (AY167598) from the spring wheat (Triticum aestivum L.) 'Avocet Susceptible' (AVS) and Xwgp-17 (AY167597) from the Yr5 near isogenic line (NIL) in the AVS background carrying the Yr5 gene from T. aestivum subsp. spelta (L.) Thell. cv. Album (TSA). Three sets of STS markers (two codominant and one dominant) were developed to amplify a region including a polymorphic 6-base pairs (bp) insertion-deletion (indel). The cosegregation of the STS markers with Yr5 was confirmed with 114 BC 7:F3 lines developed from the cross between AVS and TSA. The STS markers worked well in five out of 17 non-Yr5 wheat varieties, but the remaining varieties had a similar size of fragment to the Yr5 marker. Because the codominant STS markers were based on a 6-bp indel, they could not be separated by agarose gel electrophoresis. Cleaved amplified polymorphic sequence (CAPS) markers were then developed on the basis of a DpnII restriction site that is present in all non-Yr5 varieties and absent in the Yr5 NIL. The CAPS markers for the Yr5 NIL and non-Yr5 varieties can be separated by agarose gel electrophoresis. The codominant STS markers are easier to score than the original RGAP markers. The CAPS markers are not only easier to score, but also can be used in crosses of an Yr5 donor with a much wider range of wheat germplasms. These markers should be valuable tools to accelerate the introgression of Yr5 into commercial cultivars and to combine Yr5 with other genes for durable resistance to stripe rust

Transcriptome analysis of high-temperature adult-plant resistance conditioned by Yr39 during the wheat-Puccinia striiformis f. sp. tritici interaction

Stripe rust [caused by Puccinia striiformis Westend. f. sp. tritici Eriks. (Pst)] is a destructive disease of wheat (Triticum aestivum L.) worldwide. High-temperature adult-plant (HTAP) resistance to stripe rust is race non-specific, inherited quantitatively and durable. Previously, we identified and mapped the single Yr39 HTAP stripe rust resistance gene in the spring wheat cultivar Alpowa, which was identified on chromosome 7BL and accounted for 64.2% of the variation in resistance. To identify transcripts associated with Yr39-mediated resistance, we selected two F(7 )recombinant inbred lines (RILs) from an 'Avocet S/Alpowa' cross that differed at the Yr39 locus to represent an incompatible (Yr39) and compatible (yr39) interaction with Pst. Using the Affymetrix Wheat GeneChip, we profiled the transcript changes occurring in flag leaves of these two RILs over a time-course after treatment with Pst urediniospores and mock-inoculation. This time-course study identified 99 induced transcripts that were classified as HTAP resistance-specific. The temporal pattern of transcript accumulation showed a peak at 48 h after infection, which was supported by microscopic observation of fungal development and quantitative PCR assays that showed a rapid increase in fungal biomass after this time in the compatible interaction. More than half (50.5%) of the annotated transcripts specifically induced during HTAP resistance were involved in defence and/or signal transduction, including R gene homologues and transcripts associated with pathogenesis-related protein production, phenylpropanoid biosynthesis and protein kinase signalling. This study represents the first transcript profiling of HTAP resistance to stripe rust in wheat, and we compare our results with other transcript studies of race-specific and race non-specific resistance

Characterizing and Validating Stripe Rust Resistance Loci in US Pacific Northwest Winter Wheat Accessions (Triticum aestivum L.) by Genome‐wide Association and Linkage Mapping

Core Ideas Stripe rust resistance QTL were detected in PNW wheat panels. QTL mapping and haplotyping confirmed QYr.wac‐1B.1 and QYr.wac‐2A, and validated GWAS. SNP markers for QYr.wac‐1B.1 and for Yr17 and linked loci enable marker‐assisted selection. Stripe rust resistance is a critical need for wheat cultivars in the US Pacific Northwest (PNW). Our previous genome‐wide association study (GWAS) for stripe rust resistance in a set of PNW winter wheat accessions (Panel‐2) identified multiple marker‐trait associations (MTAs) for both all‐stage and field resistance. In this study, we conducted additional GWAS using a different set of PNW winter wheat accessions (Panel‐1) that contained recently bred soft white winter wheat breeding lines and cultivars. A total of 12 all‐stage resistance MTAs and eight field resistance MTAs were identified. Within these MTAs, nine MTAs for all‐stage resistance and two MTAs for field resistance were located distinctly from previously characterized genes and likely represent novel loci. Markers IWB60567 (1B), IWB24342 (2A), and IWB46564 (2B) explained the largest phenotypic variances for disease responses. The analysis confirmed that MTAs on chromosome 1B were indeed the same as Qyr.wpg‐1B.2 identified in Panel‐2 and that MTAs on chromosome 2A were likely Yr17 and closely linked to another field resistance QTL, Qyr.wpg‐2A.2 (Panel‐2). Haplotypes for MTAs on chromosome 1B, Yr17, and linked loci on chromosome 2A provide useful information for marker development and introgression of these QTL into wheat breeding programs