Development and utilization of single nucleotide polymorphic markers on udp-glucosyl transferases to develop Fusarium head blight resistant wheat varieties

Non-Peer Reviewe

Utilization of microsatellite markers to test purity and hybridity of canaryseed genotypes

Non-Peer Reviewe

Characterization of Arabinoxylans and β-glucans in Canadian hard red spring wheat cultivars

Non-Peer Reviewe

Analysis of nutritional composition and in-vitro enzymatic digestibility of selected rice landraces of Tamil Nadu, India

Non-Peer Reviewe

Factors Governing Pasting Properties of Waxy Wheat Flours

Citation: Purna, S. K. G., Shi, Y. C., Guan, L., Wilson, J. D., & Graybosch, R. A. (2015). Factors Governing Pasting Properties of Waxy Wheat Flours. Cereal Chemistry, 92(5), 529-535. doi:10.1094/cchem-10-14-0209-rWaxy wheat (Triticum aestivum L.) contains endosperm starch lacking in amylose. To realize the full potential of waxy wheat, the pasting properties of hard waxy wheat flours as well as factors governing the pasting properties were investigated and compared with normal and partial waxy wheat flours. Starches isolated from six hard waxy wheat flours had similar pasting properties, yet their corresponding flours had very different pasting properties. The differences in pasting properties were narrowed after endogenous alpha-amylase activity in waxy wheat flours was inhibited by silver nitrate. Upon treatment with protease, the extent of protein digestibility influenced the viscosity profile in waxy wheat flours. Waxy wheat starch granules swelled extensively when heated in water and exhibited a high peak viscosity, but they fragmented at high temperatures, resulting in more rapid breakdown in viscosity. The extensively swelled and fragmented waxy wheat starch granules were more susceptible to a-amylase degradation than normal wheat starch. A combination of endogenous a-amylase activity and protein matrix contributed to a large variation in pasting properties of waxy wheat flours

4-Phenylbutyric acid treatment rescues trafficking and processing of a mutant surfactant protein C

Mutations in the SFTPC gene, encoding surfactant protein–C (SP-C), are associated with interstitial lung disease (ILD). Knowledge of the intracellular fate of mutant SP-C is essential in the design of therapies to correct trafficking/processing of the proprotein, and to prevent the formation of cytotoxic aggregates. We assessed the potential of a chemical chaperone to correct the trafficking and processing of three disease-associated mutant SP-C proteins. HEK293 cells were stably transfected with wild-type (SP-C(WT)) or mutant (SP-C(L188Q), SP-C(Δexon4), or SP-C(I73T)) SP-C, and cell lines with a similar expression of SP-C mRNA were identified. The effects of the chemical chaperone 4-phenylbutyric acid (PBA) and lysosomotropic drugs on intracellular trafficking to the endolysosomal pathway and the subsequent conversion of SP-C proprotein to mature peptide were assessed. Despite comparable SP-C mRNA expression, proprotein concentrations varied greatly: SP-C(I73T) was more abundant than SP-C(WT) and was localized to the cell surface, whereas SP-C(Δexon4) was barely detectable. In contrast, SP-C(L188Q) and SP-C(WT) proprotein concentrations were comparable, and a small amount of SP-C(L188Q) was localized to the endolysosomal pathway. PBA treatment restored the trafficking and processing of SP-C(L188Q) to SP-C(WT) concentrations, but did not correct the mistrafficking of SP-C(I73T) or rescue SP-C(Δexon4). PBA treatment also promoted the aggregation of SP-C proproteins, including SP-C(L188Q). This study provides proof of the principle that a chemical chaperone can correct the mistrafficking and processing of a disease-associated mutant SP-C proprotein

Genetic analysis of developmental traits associated with enhanced winter survival in autumn-seeded rye (Secale cereale L.)

Non-Peer Reviewe

cDNA-AFLP analysis of cold-acclimated wheat plants reveals unique transcript profiles in crown tissues

Non-Peer ReviewedLow temperature (LT) adversely affects the productivity of plants. Hence, improving the cold hardiness of crop plants is an important goal in agriculture. However, further understanding of LT tolerance mechanisms in plants is required to achieve this objective. In wheat, survival of crown tissues after exposure to below freezing temperatures during the winter determines successful crop stand establishment at the onset of spring season. Therefore, identification of differentially expressed genes in crown tissues of cold acclimated wheat plants is important as it can allow dissection of molecular mechanisms and biochemical pathways within these tissues. In this study, cDNA-AFLP global transcriptomic profiles of crown tissues cold acclimated at 6oC for 0, 2, 14, 21, 35, 42, 56 and 70 days were compared among a cold hardy winter (vrn-A1) cv. Norstar, a tender spring habit (Vrn-A1) cv. Manitou and two reciprocal near-isogenic lines derived from these two parents differing at the vernalization locus. A total of 2061 differentially expressed transcript-derived fragments (TDFs) were identified using 37 pairs of standard AFLP primer combinations, 30 of which were considered unique due to their genotypic and temporal presence or absence. The remaining TDFs showed differential expression patterns in the four genotypes. Cluster analysis of the unique TDFs revealed influence of the genetic background on expression of these TDFs. BLAST searches of 240 sequenced TDFs showed that 87% of the TDFs had similarity to genes coding for products involved in known functions such as signal transduction, RNA processing and translation, transcription, flowering, cell wall synthesis, metabolism, and protein folding. Thirty-two TDFs did not show similarity to any known genes. Quantitative real-time PCR (QPCR) analyses of these unknown TDFs validated their differential expression patterns. Characterization of their biological function will contribute to an understanding of the role of these novel genes in LT tolerance in wheat. These results suggest that crown tissues undergo a complex adaptive process by changing the expression levels of several genes that determine the level of LT tolerance