RESUMEN
The timely degradation of tapetum, the innermost somatic anther cell layer in flowering plants, is critical for pollen development. Although several genes involved in tapetum development have been characterized, the molecular mechanisms underlying tapetum degeneration remain elusive. Here, we showed that mutation in Abnormal Degraded Tapetum 1 (ADT1) resulted in overaccumulation of Reactive Oxygen Species (ROS) and abnormal anther development, causing earlier tapetum Programmed Cell Death (PCD) and pollen abortion. ADT1 encodes a nuclear membrane localized protein, which is strongly expressed in the developing microspores and tapetal cells during early anther development. Moreover, ADT1 could interact with metallothionein MT2b, which was related to ROS scavenging and cell death regulation. These findings indicate that ADT1 is required for proper timing of tapetum PCD by regulating ROS homeostasis, expanding our understanding of the regulatory network of male reproductive development in rice.
Asunto(s)
Regulación de la Expresión Génica de las Plantas , Mutación , Oryza , Proteínas de Plantas , Polen , Especies Reactivas de Oxígeno , Oryza/genética , Oryza/crecimiento & desarrollo , Oryza/metabolismo , Polen/crecimiento & desarrollo , Polen/genética , Especies Reactivas de Oxígeno/metabolismo , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Muerte Celular , Flores/crecimiento & desarrollo , Flores/genética , ApoptosisRESUMEN
The leaf is the main site of photosynthesis and is an important component in shaping the ideal rice plant architecture. Research on leaf morphology and development will lay the foundation for high-yield rice breeding. In this study, we isolated and identified a novel curling leaf mutant, designated curling leaf 1 (cl1). The cl1 mutant exhibited an inward curling phenotype because of the defective development of sclerenchymatous cells on the abaxial side. Meanwhile, the cl1 mutant showed significant reductions in grain yield and thousand-grain weight due to abnormal leaf development. Through map-based cloning, we identified the CL1 gene, which encodes a MYB transcription factor that is highly expressed in leaves. Subcellular localization studies confirmed its typical nuclear localization. Transcriptome analysis revealed a significant differential expression of the genes involved in photosynthesis, leaf morphology, yield formation, and hormone metabolism in the cl1 mutant. Yeast two-hybrid assays demonstrated that CL1 interacts with alpha-tubulin protein SRS5 and AP2/ERF protein MFS. These findings provide theoretical foundations for further elucidating the mechanisms of CL1 in regulating leaf morphology and offer genetic resources for practical applications in high-yield rice breeding.
RESUMEN
Catalase (CAT) is an important antioxidant enzyme in plants that plays a key role in plant growth and stress responses. CAT is usually encoded by a small gene family that has been cloned and functionally studied in some species, such as Arabidopsis, wheat and cucumber, but its specific roles in rice are not clear at present. In this study, we identified three CAT family genes (OsCAT1, OsCAT2 and OsCAT3) in the rice genome and performed a systematic bioinformatics analysis. RT-PCR analysis revealed that OsCAT1-OsCAT3 was primarily expressed in vegetative tissues such as roots, stems and leaves. Since OsCAT3 showed the highest expression level among the three OsCAT genes, we then focused on its related functions. OsCAT3 prokaryotic expression protein has an obvious ability to remove H2O2. The OsCAT3crispr plant was short and had a low survival rate, the leaves were small with brown lesions, and the activities of the CAT, POD and SOD enzymes were significantly reduced. A microarray analysis showed that differentially expressed genes were primarily enriched in toxin metabolism and photosynthesis. This study laid a foundation for further understanding the function of the rice OsCAT gene.
Asunto(s)
Oryza , Catalasa/genética , Catalasa/metabolismo , Peróxido de Hidrógeno/metabolismo , Antioxidantes/metabolismo , FotosíntesisRESUMEN
Enzyme-catalyzed radical-mediated C-H functionalization reactions allow nature to create natural products of unusual three-dimensional structures from simple linear peptide precursors. In comparison, chemist's ability to harness radical C-H functionalization reactions for synthesis of complex peptides remains limited. In this work, new methods have been developed to construct peptide macrocycles via radical-mediated intramolecular C-H alkylation reactions under photoredox catalysis. Linear peptide precursors equipped with a C-terminal N-(acyloxy)phthalimide ester can cyclize with the α C-H bond of N-terminal glycine or aryl C-H bond of N-heteroarene capping units in high yield and selectivity under mild conditions. The strategy uses the C-H cyclization step to incorporate lysine, homolysine, and various heteroarene-derived amino acid linchpins into peptide macrocycles, enabling convergent and flexible synthesis of complex peptide macrocycles from simple building blocks.
Asunto(s)
Péptidos Cíclicos/química , Péptidos/química , Alquilación , Catálisis , Ciclización , Estructura MolecularRESUMEN
We report an efficient and economical method for remote δ C(sp3)-H heteroarylation of free aliphatic alcohols using a hypervalent iodine PFBI-OH oxidant under photoredox catalysis. The reaction sequence involves in situ alcoholysis of PFBI-OH with alcohol, generation of an alkoxy radical intermediate by SET reduction, 1,5-HAT, and Minisci-type C-C bond formation. This method uses a slight excess of alcohols, can facilitate reaction at δ methyl and methylene positions, and has been successfully applied to modification of complex drug molecules.
RESUMEN
Reversible cleavage of C(sp3)-H bonds can enable racemization or epimerization, offering a valuable tool to edit the stereochemistry of organic compounds. While epimerization reactions operating via cleavage of acidic C(sp3)-H bonds, such as the Cα-H of carbonyl compounds, have been widely used in organic synthesis and enzyme-catalyzed biosynthesis, epimerization of tertiary carbons bearing a nonacidic C(sp3)-H bond is much more challenging with few practical methods available. Herein, we report the first synthetically useful protocol for the epimerization of tertiary carbons via reversible radical cleavage of unactivated C(sp3)-H bonds with hypervalent iodine reagent benziodoxole azide and H2O under mild conditions. These reactions exhibit excellent reactivity and selectivity for unactivated 3° C-H bonds of various cycloalkanes and offer a powerful strategy for editing the stereochemical configurations of carbon scaffolds intractable to conventional methods. Mechanistic study suggests that the unique ability of N3⢠to serve as a catalytic H atom shuttle is critical to reversibly break and reform 3° C-H bonds with high efficiency and selectivity.