Identification of intergeneric and synthetic spring wheat lines with resistance to Fusarium head blight

Non-Peer ReviewedFusarium head blight (FHB) is a serious disease in many cereal crops worldwide, as it can drastically reduce both yield and quality in infected crops. Resistance to FHB is therefore a desirable trait for incorporation into new wheat cultivars. Wild relatives are a source of new genetic variation and have been shown to enhance disease resistance when hybridized with wheat. This research has focused on evaluating intergeneric and interspecific wheat lines for resistance to FHB. Intergeneric hybrids of wheat (Triticum aestivum) and Agropyron repens syn. Elytrigia repens, and synthetic wheat lines produced at CIMMYT, were evaluated under greenhouse conditions for resistance to FHB caused by Fusarium graminearum. Approximately 35% of the intergeneric lines and 15% of the synthetic lines consistently displayed moderate to high levels of Type II resistance. Pollen staining was conducted to determine the fertility levels of the intergeneric lines. 79% of the F3 lines and 72% of the F5 and F6 lines displayed fertility levels above 75%. Control cultivars displayed fertility levels ranging from 88-94%. Generally, lines that rated as moderately to highly resistant were also highly fertile. These lines could be of significant value in wheat breeding programs aimed at integrating new sources of resistance to Fusarium head blight

The yeast ER-intramembrane protease Ypf1 refines nutrient sensing by regulating transporter abundance.

Proteolysis by aspartyl intramembrane proteases such as presenilin and signal peptide peptidase (SPP) underlies many cellular processes in health and disease. Saccharomyces cerevisiae encodes a homolog that we named yeast presenilin fold 1 (Ypf1), which we verify to be an SPP-type protease that localizes to the endoplasmic reticulum (ER). Our work shows that Ypf1 functionally interacts with the ER-associated degradation (ERAD) factors Dfm1 and Doa10 to regulate the abundance of nutrient transporters by degradation. We demonstrate how this noncanonical branch of the ERAD pathway, which we termed "ERAD regulatory" (ERAD-R), responds to ligand-mediated sensing as a trigger. More generally, we show that Ypf1-mediated posttranslational regulation of plasma membrane transporters is indispensible for early sensing and adaptation to nutrient depletion. The combination of systematic analysis alongside mechanistic details uncovers a broad role of intramembrane proteolysis in regulating secretome dynamics