The aim of this study was to explore the molecular mechanisms of induced leaf senescence by preventing pollination in maize using a proteomic method combined with other physiological methods. An elite maize inbred line Yu816 was selected for evaluation of its senescence mechanism. Phenotypic and chlorophyll content analysis revealed that the onset of leaf senescence occurred earlier in non-pollinated (NONPOL) leaves than pollinated (POL) leaves. Leaf protein species of NONPOL and POL leaves were separately extracted and their proteomes were assessed using isobaric tags for relative and absolute quantitation (iTRAQ) analysis. A total of 4371 protein species were identified, of which 809 exhibited differentially altered abundance (P < 0.05). The identified protein species were related to diverse functions including photosystems, plant hormones, cell death, oxidative degradation, and protein metabolism, suggesting a potential signaling cascade for ear leaf senescence induced by pollination prevention. In addition, leaf total soluble sugar and leaf starch contents were remarkably higher in NONPOL plants than in POL plants. These findings suggest that induced leaf senescence might be associated with nutrient remobilization. Our results reveal a network of molecular mechanisms at the protein level and provide some insights into the early senescence mechanism in higher plants. Biological significance: The coordination between growth and timing for senescence is critical for maize production. However, the molecular mechanism of induced leaf senescence by preventing pollination in maize remains to be further elucidated at the proteomic level. Herein, we revealed some new protein species that are involved in hormone signaling, glycometabolism, oxidation-reduction, protein degradation and photosystem breakdown, and other biological processes that were not previously known to be associated with leaf senescence. This is the first large-scale proteomics study to examine induced leaf senescence in maize by preventing pollination.
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http://dx.doi.org/10.1016/j.jprot.2018.02.017 | DOI Listing |
Plant Physiol Biochem
December 2024
College of Bioscience and Biotechnology, Shenyang Agricultural University, Shenyang, 110866, China; Key Laboratory of Fruit and Vegetable Biology and Germplasm Enhancement, Shenyang Agricultural University, Shenyang, 110866, China; Key Laboratory of Protected Horticulture of Ministry of Education, Shenyang Agricultural University, Shenyang, 110866, China. Electronic address:
SnRK1 (SNF1-related kinase 1), a member of the SNF1 protein kinase superfamily, has been demonstrated to play a role in plant growth and development, as well as in stress responses. In this experiment, the leaf senescence of 'Xintaimici' cucumber was simulated by dark treatment and studied using SnRK1 activator/inhibitor and transient transformation technology. The effects of SnRK1 on cucumber leaf senescence, reactive oxygen species (ROS) metabolism, chloroplast structure, and photosynthetic characteristics were studied.
View Article and Find Full Text PDFJ Food Drug Anal
December 2024
School of Pharmacy, Naval Medical University, Shanghai, 200433, China.
Bitter acids (BA) are main component of Humulus lupulus L. (hops). They are known for beer brewing and have various biological and pharmacological properties, especially the bone-protective effect confirmed by our previous in vivo study.
View Article and Find Full Text PDFPLoS One
January 2025
Department of Biology, The Pennsylvania State University, University Park, PA, United States of America.
J Agric Food Chem
January 2025
School of Food and Biological Engineering, Hefei University of Technology, Hefei 230009, China.
A nuclear-localized cysteine desulfhydrase, LCD1, plays a crucial role in mediating endogenous hydrogen sulfide production in tomatoes. However, the mechanism underlying the nuclear localization of SlLCD1 is not yet fully understood. In this study, it was found that SlLCD1 specifically interacted with nuclear import receptor importin α3 (SlIMPA3).
View Article and Find Full Text PDFPlant Cell Rep
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Floriculture Lab, Agrotechnology Division, CSIR-Institute of Himalayan Bioresource Technology, (CSIR-IHBT), Palampur, H.P., 176061, India.
Everlastin1 and Everlastin2, potent inhibitors of EPH1, were identified through a wheat cell-free chemical-screening system. This innovative platform enables the development of small molecules that target 'undruggable' transcription factors. By specifically targeting the EPH1 pathway, these inhibitors delay petal senescence, extending the longevity and quality of ornamental flowers.
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