Rice feeds half the world's population, and rice blast is often a destructive disease that results in significant crop loss. Non-race-specific resistance has been more effective in controlling crop diseases than race-specific resistance because of its broad spectrum and durability. Through a genome-wide association study, we report the identification of a natural allele of a CH-type transcription factor in rice that confers non-race-specific resistance to blast. A survey of 3,000 sequenced rice genomes reveals that this allele exists in 10% of rice, suggesting that this favorable trait has been selected through breeding. This allele causes a single nucleotide change in the promoter of the bsr-d1 gene, which results in reduced expression of the gene through the binding of the repressive MYB transcription factor and, consequently, an inhibition of HO degradation and enhanced disease resistance. Our discovery highlights this novel allele as a strategy for breeding durable resistance in rice.

Cortactin, a filamentous actin cross-linking protein and a substrate of Src protein tyrosine kinase, is phosphorylated at tyrosine residues upon stimulation by extracellular signals. We have previously demonstrated that the filamentous actin cross-linking activity of cortactin is attenuated by Src (Huang, C., Ni, Y., Gao, Y., Haudenschild, C. C., and Zhan, X. (1997) J. Biol. Chem. 272, 13911-13915).In vitro, tyrosine phosphorylation of cortactin occurs specifically within the region between the proline-rich sequence and the Src homology 3 domain. Among the nine tyrosine residues in this region, mutations at Tyr 421 , Tyr 466 , and Tyr 482 significantly reduced Src-meditated tyrosine phosphorylation both in vitro and in vivo. Ectopic expression of wild-type cortactin in ECV304, a spontaneously transformed human umbilical endothelial cell line, resulted in an enhanced cell migration. In contrast, overexpression of a cortactin mutant deficient in tyrosine phosphorylation impaired the migration of endothelial cells. These findings reveal an intracellular signaling mechanism whereby the motility of endothelial cells is regulated by a Src-mediated tyrosine phosphorylation of cortactin.Endothelial cells, which line the lumen of blood vessels, are versatile in morphology and undergo a rapid remodeling during vascularization. Whereas the mechanism for remodeling endothelial cells is not fully understood, the stimulation of the cytoskeletal reorganization that begins underneath the plasma membrane by extracellular signals, especially angiogenic factors, is likely to play an important role in physiological and pathological functions of endothelial cells such as angiogenesis (1).In a previous effort to characterize signaling molecules of fibroblast growth factor 1 (FGF-1), 1 a potent endothelial cell growth factor, we identified a phosphotyrosyl protein as cortactin, a substrate of Src protein tyrosine kinase (2). Tyrosine phosphorylation of cortactin induced by FGF-1 is elevated during the late G 1 phase (4 -6 h) in Balb 3T3 fibroblasts. The stimulation with FGF-1 also results in a transient association of Src with cortactin as well as in an association of FGF receptor 1 with Src (3), suggesting that the activation of Src is a mechanism for the tyrosine phosphorylation of cortactin induced by FGF-1. In addition to FGF-1, various other extracellular stimuli, which often result in a cell motility response, also stimulate the tyrosine phosphorylation of cortactin. These signals include epidermal growth factor (4), thrombin (5), collagen (6), integrin activation (7, 8), phagocytosis (9), and mechanical strain (10).The protein sequence of cortactin features a unique structure characterized by six and a half 37-amino acid tandem repeats and a Src homology 3 (SH3) domain at the carboxyl terminus. Between the SH3 and the repeat domains are an ␣-helical structure and a sequence rich in proline residues. This structural feature containing a repeat domain and a carboxyl-terminal SH3 domain resembles neufectin, a F-actin-associated pr...

Following our recent study demonstrating predominant Li-ion hopping conduction in sulfolane (SL)-based highly concentrated electrolytes with LiBF4, LiClO4, and lithium bis­(fluorosulfonyl)­amide, herein a systematic study on transport properties and Li-ion coordination of SL-based electrolytes with lithium bis­(trifluoromethanesulfonyl)­amide was performed. In the highly concentrated region, Li ions clearly diffuse faster than SL and TFSA anions. The two oxygen atoms of the SL sulfonyl group tend to coordinate to two different neighboring Li ions and TFSA anions form ionic clusters with Li ions, verifying the previous observation of the unusual Li-ion conduction and its relevance to the SL- and anion-bridged, chainlike Li-ion coordination structure for the SL-based concentrated systems with other Li salts. Moreover, addition of hydrofluoroether (HFE) to the SL-based concentrated electrolytes greatly enhances diffusion coefficients but fragments the chainlike Li-ion coordination to smaller clusters, leading to a reduced contribution of Li-ion hopping to the overall Li-ion conduction. The SL-based concentrated electrolyte and its mixtures with HFE showed lower lithium polysulfide solubility and higher rate capability for lithium–sulfur (Li–S) cells compared with previously reported tetraglyme-based electrolytes. The SL-based electrolytes were found to manifest a significant improvement in Li-ion mass transfer as a sparingly solvating electrolyte, enabling the solid-state sulfur redox reactions in high-performance Li–S batteries.

Plant immunity often penalizes growth and yield. The transcription factor Ideal Plant Architecture 1 (IPA1) reduces unproductive tillers and increases grains per panicle, which results in improved rice yield. Here we report that higher IPA1 levels enhance immunity. Mechanistically, phosphorylation of IPA1 at amino acid Ser within its DNA binding domain occurs in response to infection by the fungus and alters the DNA binding specificity of IPA1. Phosphorylated IPA1 binds to the promoter of the pathogen defense gene and activates its expression, leading to enhanced disease resistance. IPA1 returns to a nonphosphorylated state within 48 hours after infection, resuming support of the growth needed for high yield. Thus, IPA1 promotes both yield and disease resistance by sustaining a balance between growth and immunity.