Protein ubiquitination, which is a major post-translational modifications that occurs in eukaryotic cells, is involved in diverse biological processes. To date, large-scale profiling of the ubiquitome in common wheat has not been reported, despite its status as the major cereal crop in the world. Here, we performed the first ubiquitome analysis of the common wheat (Triticum aestivum L.) variety, Aikang 58. Overall, 433 lysine modification sites were identified in 285 proteins in wheat seedlings, and four putative ubiquitination motifs were revealed. In particular, 83 of the 285 ubiquitinated proteins had ubiquitination orthologs in Oryza sativa L., and Arabidopsis thaliana. Ubiquitylated lysines were found to have a significantly different preference for secondary structures when compared with the all lysines. In accordance with previous studies, proteins related to binding and catalytic activity were predicted to be the preferential targets of lysine ubiquitination. Besides, protein interaction network analysis reveals that diverse interactions are modulated by protein ubiquitination. Bioinformatics analysis revealed that the ubiquitinated proteins were involved in diverse biological processes. Our data provides a global view of the ubiquitome in common wheat for the first time and lays a foundation for exploring the physiological role of lysine ubiquitination in wheat and other plants.
Plasma membrane-associated abscisic acid (ABA) signal transduction is an integral part of ABA signaling. The C2-domain ABA-related (CAR) proteins play important roles in the recruitment of ABA receptors to the plasma membrane to facilitate ABA signaling. However, how CAR proteins are regulated remains unclear. In this study, we conducted a genetic screen for mutants with altered leaf transpiration and identified an uncharacterized protein, LOWER TEMPERATURE 1 (LOT1), which regulates the dynamic localization and stability of CAR proteins. The lot1 mutant had a lower leaf temperature as compared with the wild type due to higher transpiration. We found that LOT1 physically interacts with CAR9 , and ABA reduces LOT1-CAR9 interaction in the nucleus, likely via Ca 2+ , resulting in increased localization of CAR9 to the plasma membrane. We further found that the stability of CAR9 is affected by LOT1 less CAR9 proteins were accumulated and more were ubiquitinated in lot1. While the lot1, car9 and lot1 car9 mutants were hyposensitive to ABA, the hyposensitive phenotype of lot1 could be rescued by CAR9 overexpression. Collectively, our study reveals that LOT1 regulates plant tolerance to drought stress by affecting ABA signaling through regulating the stability and dynamic localization of CAR9.
Summary
Riboflavin is the precursor of essential cofactors for diverse metabolic processes. Unlike animals, plants can de novo produce riboflavin through an ancestrally conserved pathway, like bacteria and fungi. However, the mechanism by which riboflavin regulates seed development is poorly understood. Here, we report a novel maize (Zea mays L.) opaque mutant o18, which displays an increase in lysine accumulation, but impaired endosperm filling and embryo development. O18 encodes a rate‐limiting bifunctional enzyme ZmRIBA1, targeted to plastid where to initiate riboflavin biosynthesis. Loss of function of O18 specifically disrupts respiratory complexes I and II, but also decreases SDH1 flavinylation, and in turn shifts the mitochondrial tricarboxylic acid (TCA) cycle to glycolysis. The deprivation of cellular energy leads to cell‐cycle arrest at G1 and S phases in both mitosis and endoreduplication during endosperm development. The unexpected up‐regulation of cell‐cycle genes in o18 correlates with the increase of H3K4me3 levels, revealing a possible H3K4me‐mediated epigenetic back‐up mechanism for cell‐cycle progression under unfavourable circumstances. Overexpression of O18 increases riboflavin production and confers osmotic tolerance. Altogether, our results substantiate a key role of riboflavin in coordinating cellular energy and cell cycle to modulate maize endosperm development.
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