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1.
Biotechnol Adv ; 32(2): 390-402, 2014.
Artículo en Inglés | MEDLINE | ID: mdl-24389085

RESUMEN

The ascomycete fungus, Fusarium graminearum (teleomorph Gibberella zeae), is the most common causal agent of Fusarium head blight (FHB), a devastating disease for cereal crops worldwide. F. graminearum produces ascospores (sexual spores) and conidia (asexual spores), which can serve as disease inocula of FHB. Meanwhile, Fusarium-infected grains are often contaminated with mycotoxins such as trichothecenes (TRIs), fumonisins, and zearalenones, among which TRIs are related to the pathogenicity of F. graminearum, and these toxins are hazardous to humans and livestock. In recent years, with the complete genome sequencing of F. graminearum, an increasing number of functional genes involved in the production of secondary metabolites, hyphal differentiation, sexual and asexual reproduction, virulence and pathogenicity have been identified from F. graminearum. In this review, the secondary metabolite synthesis, hyphal development and pathogenicity related genes in F. graminearum were thoroughly summarized, and the genes associated with secondary metabolites, sexual reproduction, energy metabolism, and pathogenicity were highlighted.


Asunto(s)
Fusarium , Genes Fúngicos/genética , Gibberella , Fusarium/genética , Fusarium/metabolismo , Fusarium/patogenicidad , Fusarium/fisiología , Gibberella/genética , Gibberella/metabolismo , Gibberella/patogenicidad , Gibberella/fisiología , Virulencia
2.
Appl Microbiol Biotechnol ; 97(18): 7977-87, 2013 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-23917634

RESUMEN

Proteins that serve as regulator of G protein signaling (RGS) primarily function as GTPase accelerators that promote GTP hydrolysis by the Gα subunits, thereby inactivating the G protein and rapidly switching off G protein-coupled signaling pathways. Since the first RGS protein was identified from the budding yeast Saccharomyces cerevisiae, more than 30 RGS and RGS-like proteins have been characterized from several model fungi, such as Aspergillus nidulans, Beauveria bassiana, Candida albicans, Fusarium verticillioides, Magnaporthe oryzae, and Metarhizium anisopliae. In this review, the partial biochemical properties and functional domains of RGS and RGS-like proteins were predicted and compared, and the roles of RGS and RGS-like proteins in different fungi were summarized. Moreover, the phylogenetic relationship among RGS and RGS-like proteins from various fungi was analyzed and discussed.


Asunto(s)
Proteínas Fúngicas/metabolismo , Hongos/metabolismo , Proteínas RGS/metabolismo , Proteínas Fúngicas/química , Proteínas Fúngicas/genética , Hongos/química , Hongos/clasificación , Hongos/genética , Filogenia , Proteínas RGS/química , Proteínas RGS/genética
3.
Arch Microbiol ; 195(7): 453-62, 2013 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-23661195

RESUMEN

Nematode-trapping fungi can secrete many extracellular hydrolytic enzymes such as serine proteases and chitinases to digest and penetrate nematode/egg-cuticles. However, little is known about the structure and function of chitinases in these fungi. In this study, 16 ORFs encoding putative chitinases, which all belong to glycoside hydrolase (GH) family 18, were identified from the Arthrobotrys oligospora genome. Bioinformatics analyses showed that these 16 putative chitinases differ in their functional domains, molecular weights and pI. Phylogenetic analysis grouped these A. oligospora chitinases into four clades: clades I, II, III and IV, respectively, including an A. oligospora-specific subclade (Clade IV-B) that contained high-molecular weight chitinases (≥100 kDa). Transcriptional analysis of A. oligospora chitinases suggested that the expression of most chitinases was repressed by carbon starvation, and all chitinases were up-regulated under nitrogen starvation. However, chitinase AO-190 was up-regulated under carbon and/or nitrogen starvation. Moreover, several chitinases (such as AO-59, AO-190 and AO-801) were up-regulated in the presence of chitinous substrates or a plant pathogenic fungus, indicating that they could play a role in biocontrol applications of A. oligospora. Our results provided a basis for further understanding the functions, diversities and evolutionary relationships between chitinase genes in nematode-trapping fungi.


Asunto(s)
Ascomicetos/enzimología , Ascomicetos/genética , Quitinasas/genética , Secuencia de Aminoácidos , Animales , Ascomicetos/fisiología , Quitinasas/química , Quitinasas/metabolismo , Proteínas Fúngicas/química , Proteínas Fúngicas/genética , Proteínas Fúngicas/metabolismo , Regulación Fúngica de la Expresión Génica , Genes Fúngicos , Datos de Secuencia Molecular , Peso Molecular , Nematodos/microbiología , Sistemas de Lectura Abierta , Filogenia , Estructura Terciaria de Proteína , Transcripción Genética
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