Genética de la resistencia al complejo mancha de asfalto en 18 genotipos tropicales de maíz

George Mahuku Ignacio Benítez-Riquelme Serafin Cruz-Izquierdo (2015, [Artículo])

Horizontal Resistance Tar Spot Complex CIENCIAS AGROPECUARIAS Y BIOTECNOLOGÍA FUNGI MONOGRAPHELLA PHYLLACHORALES ZEA MAYS DIALLEL ANALYSIS DISEASE RESISTANCE

Coinfection and in vitro interaction of Lasiodiplodia pseudotheobromae and Pestalotiopsis mangiferae associated with dieback in branches of mango (Mangifera indica) Manila variety, in Veracruz, Mexico

LILIANA EUNICE SAUCEDO PICAZO Luis Guillermo Hernández Montiel NORMA FLORES ESTEVEZ PATRICIA GEREZ FERNANDEZ ANGEL FERNANDO ARGÜELLO ORTIZ JUAN CARLOS NOA CARRAZANA (2022, [Artículo])

"Dieback disease caused by fungal complexes is a severe problem in mango trees (Mangifera indica). Its main symptoms are branch rot, gummosis, and finally, the tree’s death. In this work, the species of the fungal complex causing mango dieback in the Manila variety in Veracruz, Mexico were identified. The in vitro interaction of two species belonging to the complex was evaluated and the severity of the co-infection in mango branches. Lasiodiplodia pseudotheobromae and Pestalotiopsis mangiferae were identified as causal agents of mango dieback in the producing area of Veracruz. In coinfected mango branches, greater severity of necrosis was observed than in individual infections. Liquid culture filtrates applied in co-cultures showed different results for each species of phytopathogen. The P. mangiferae filtrate had no significant antagonistic effects on the growth of L. pseudotheobromae (inhibition of 2.68%), while the L. pseudotheobromae filtrate inhibited 41.38% of P. mangiferae. The results show that multiple infections in mango trees increase the damage caused by dieback, which could directly impact the development of control strategies."

gummosis, virulence, interaction, fungal complex CIENCIAS AGROPECUARIAS Y BIOTECNOLOGÍA CIENCIAS AGRARIAS FITOPATOLOGÍA FITOPATOLOGÍA FITOPATOLOGÍA

Coronin is a component of the endocytic collar of hyphae of neurospora crassa and is necessary for normal growth and morphogenesis

RAMON OSVALDO ECHAURI ESPINOSA (2012, [Artículo])

Coronin plays a major role in the organization and dynamics of actin in yeast. To investigate the role of coronin in a filamentous fungus (Neurospora crassa), we examined its subcellular localization using fluorescent proteins and the phenotypic consequences of coronin gene (crn-1) deletion in hyphal morphogenesis, Spitzenkörper behavior and endocytosis. Coronin-GFP was localized in patches, forming a subapical collar near the hyphal apex; significantly, it was absent from the apex. The subapical patches of coronin colocalized with fimbrin, Arp2/3 complex, and actin, altogether comprising the endocytic collar. Deletion of crn-1 resulted in reduced hyphal growth rates, distorted hyphal morphology, uneven wall thickness, and delayed establishment of polarity during germination; it also affected growth directionality and increased branching. The Spitzenkörper of Δcrn-1 mutant was unstable; it appeared and disappeared intermittently giving rise to periods of hyphoid-like and isotropic growth respectively. Uptake of FM4-64 in Δcrn-1 mutant indicated a partial disruption in endocytosis. These observations underscore coronin as an important component of F-actin remodeling in N. crassa. Although coronin is not essential in this fungus, its deletion influenced negatively the operation of the actin cytoskeleton involved in the orderly deployment of the apical growth apparatus, thus preventing normal hyphal growth and morphogenesis. © 2012 Echauri-Espinosa et al.

actin related protein 2-3 complex, F actin, fimbrin protein, fluorescent dye, fungal protein, fungal protein coronin, green fluorescent protein, unclassified drug, actin binding protein, coronin proteins, fungal protein, article, cell polarity, contr BIOLOGÍA Y QUÍMICA CIENCIAS DE LA VIDA MICROBIOLOGÍA MICROBIOLOGÍA

Functional characterization and cellular dynamics of the CDC-42 - RAC - CDC-24 module in neurospora crassa

CYNTHIA LIZZETH ARAUJO PALOMARES (2011, [Artículo])

Rho-type GTPases are key regulators that control eukaryotic cell polarity, but their role in fungal morphogenesis is only beginning to emerge. In this study, we investigate the role of the CDC-42 - RAC - CDC-24 module in Neurospora crassa. rac and cdc-42 deletion mutants are viable, but generate highly compact colonies with severe morphological defects. Double mutants carrying conditional and loss of function alleles of rac and cdc-42 are lethal, indicating that both GTPases share at least one common essential function. The defects of the GTPase mutants are phenocopied by deletion and conditional alleles of the guanine exchange factor (GEF) cdc-24, and in vitro GDP-GTP exchange assays identify CDC-24 as specific GEF for both CDC-42 and RAC. In vivo confocal microscopy shows that this module is organized as membrane-associated cap that covers the hyphal apex. However, the specific localization patterns of the three proteins are distinct, indicating different functions of RAC and CDC-42 within the hyphal tip. CDC-42 localized as confined apical membrane-associated crescent, while RAC labeled a membrane-associated ring excluding the region labeled by CDC42. The GEF CDC-24 occupied a strategic position, localizing as broad apical membrane-associated crescent and in the apical cytosol excluding the Spitzenkörper. RAC and CDC-42 also display distinct localization patterns during branch initiation and germ tube formation, with CDC-42 accumulating at the plasma membrane before RAC. Together with the distinct cellular defects of rac and cdc-42 mutants, these localizations suggest that CDC-42 is more important for polarity establishment, while the primary function of RAC may be maintaining polarity. In summary, this study identifies CDC-24 as essential regulator for RAC and CDC-42 that have common and distinct functions during polarity establishment and maintenance of cell polarity in N. crassa. © 2011 Araujo-Palomares et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

CDC24 protein, guanine nucleotide exchange factor, protein Cdc42, Rac protein, unclassified drug, cell cycle protein, fungal protein, membrane protein, multiprotein complex, protein Cdc42, Rac protein, allele, apical membrane, article, assay, cell me BIOLOGÍA Y QUÍMICA CIENCIAS DE LA VIDA MICROBIOLOGÍA MICROBIOLOGÍA