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  • Open Access

    ARTICLE

    Aggressiveness Assessment of Two Fusarium spp. on Durum Wheat Grain Coleoptiles under Controlled Conditions

    Salah Hadjout1,2,*, Mohamed Zouidi1, Houcine Bougrine1, Abdeldjalil Belkendil1, Amer Zeghmar1, Walid Ouaret3, Walid Soufan4, Fathi Abdellatif Belhouadjeb5

    Phyton-International Journal of Experimental Botany, Vol.93, No.11, pp. 2983-2992, 2024, DOI:10.32604/phyton.2024.056982 - 30 November 2024

    Abstract Fusarium head blight (FHB) is a disease caused by several Fusarium species, notably, F. culmorum and F. graminearum. These pathogens adversely affect the technological and sanitary qualities of cereal grains, particularly durum wheat. Under favorable environmental conditions and in susceptible varieties, these Fusarium species can significantly reduce both the quantity and quality of crops. This study evaluated the pathogenicity of the two Fusarium species (FC2006 and FG2008) in the growth of durum wheat coleoptiles. The plant material included four commercially grown parental varieties (G9, G10, G11, G12) and eight breeding lines (G1, G2, G3, G4, G5, G6, G7, G8).… More >

  • Open Access

    ARTICLE

    Apparent cross-talk of two signaling pathways that regulate Zea mays coleoptile growth

    Buentello Volante1 B, F Díaz de León-Sánchez1, F Rivera-Cabrera1, R Aguilar Caballero2, M Ponce-Valadez1, E Sánchez de Jiménez2, LJ Pérez-F lores1

    Phyton-International Journal of Experimental Botany, Vol.79, pp. 101-108, 2010, DOI:10.32604/phyton.2010.79.101

    Abstract Auxin and insulin promote Zea mays embryo growth, induce S6 ribosomal protein (S6rp) phosphorylation, and promote specific protein synthesis. The objective of this research was to test a possible cross-talk between insulin and auxin transduction pathways in Z. mays coleoptiles, typical auxin target tissues. Auxin and insulin produced differential quantitative and qualitative stimulation of cytoplasmic and ribosomal protein phosphorylation, and specific patterns of de novo synthesized cytoplasmic proteins. In addition, insulin induced S6rp phosphorylation was strongly inhibited by rapamycin, indicating target of rapamycin (TOR) kinase participation; auxin-induced S6rp phosphorylation was insensitive to this inhibitor. Phosphatidic acid (PA), a More >

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