The root knot nematodes (RKN), spp., particularly and species, parasitize several plant species and are responsible for large annual yield losses all over the world. Only a few available chemical nematicides are still authorized for RKN control owing to environmental and health reasons. Thus, plant resistance is currently considered the method of choice for controlling RKN, and research performed on the molecular interactions between plants and nematodes to identify genes of interest is of paramount importance. The present work aimed to identify the differential accumulation of root proteins of a resistant cowpea genotype (CE-31) inoculated with (Race 3) in comparison with mock-inoculated control, using 2D electrophoresis assay, mass spectrometry identification and gene expression analyses by RT-PCR. The results showed that at least 22 proteins were differentially represented in response to RKN challenge of cowpea roots mainly within 4-6 days after inoculation. Amongst the up-represented proteins were SOD, APX, PR-1, β-1,3-glucanase, chitinases, cysteine protease, secondary metabolism enzymes, key enzymes involved in ethylene biosynthesis, proteins involved in MAPK pathway signaling and, surprisingly, leghemoglobin in non-rhizobium-bacterized cowpea. These findings show that an important rearrangement in the resistant cowpea root proteome occurred following challenge with .
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http://dx.doi.org/10.3390/proteomes2040527 | DOI Listing |
Toxics
December 2024
Department of Industrial Engineering, University of Applied Sciences Technikum Wien, 17 Hoechstaedtplatz 6, 1200 Vienna, Austria.
Cadmium (Cd) is one of the foremost phytotoxic elements. Its proportion in agricultural soil is increasing critically due to anthropogenic activities. Cd stress is a major crop production threat affecting food security globally.
View Article and Find Full Text PDFMol Biol Rep
November 2024
School of Environmental and Municipal Engineering, Lanzhou Jiaotong University, Lanzhou, 730070, P.R. China.
Background: Cytochrome c oxidase (COX) is a crucial mitochondrial enzyme in the electron transport chain of plants, implicated in energy production and stress responses. Despite its importance, the function of COX in leguminous plants, especially under heavy metal stress like cadmium (Cd), remains understudied.
Methods And Results: In this study, COX genes (COX s) were identified based on the genome annotation file in mung bean (Vigna radiata (Linn.
Plant Dis
November 2024
University of Hawaii, Plant and Environmental Protection Sciences, 3050 Maile Way #310, Honolulu, Hawaii, United States, 96822;
J Hazard Mater
December 2024
Guangdong Key Laboratory of Integrated Agro-Environmental Pollution Control and Management, Institute of Eco-environmental and Soil Sciences, Guangdong Academy of Sciences, Guangzhou 510650, Guangdong, PR China.
In this study, Cd isotope analysis was conducted on drought-tolerant (cowpea and sesame) and less drought-tolerant vegetables (water spinach, green pepper, and mung bean) to elucidate the mechanisms underlying Cd uptake and transport. Cd isotopes in plants were identical to or lighter than those in the available pool and exhibited negative fractionation from roots to straws (ΔCd = -0.22 ‰ to -0.
View Article and Find Full Text PDFBiochem Biophys Res Commun
December 2024
Department of Biochemistry and Biotechnology, Plant and Environmental Biotechnology Laboratory, University of Thessaly, Viopolis, Larissa, 41500, Greece. Electronic address:
Oxidosqualene cyclases (OSCs) are important regulatory enzymes involved in cyclization reactions of 2, 3-oxidosqualene to form triterpenes and sterols. This study presents the identification and characterization of three OSC genes, a β - amyrin synthase (VuβAS), a lupeol synthase (VuLUS) and a cycloartenol synthase (VuCAS) in Vigna unguiculata, an edible leguminous plant with high nutritional and nutraceutical value. Phylogenetic analysis showed that the VuβAS, VuLUS and VuCAS were clustered within the clades of previously characterized β - amyrin synthases, lupeol synthases and cycloartenol synthases.
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