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1.
Biochem Biophys Res Commun ; 297(5): 1197-204, 2002 Oct 11.
Artigo em Inglês | MEDLINE | ID: mdl-12372414

RESUMO

Tetraspanins are animal proteins involved in membrane complexes that are involved in cell adhesion, differentiation, and motility. The PLS1 gene from rice blast fungus Magnaporthe grisea encodes a protein (Pls1p) structurally related to tetraspanins that is required for pathogenicity. In Botrytis cinerea public sequences, we identified an EST homologous to PLS1. Using degenerated oligonucleotides, we amplified sequences homologous to PLS1 in fungi Colletotrichum lindemuthianum and Neurospora crassa. Analysis of N. crassa and M. grisea genome sequences revealed the presence of a single tetraspanin gene. Thus, fungi differ from animals, which contain between 20 and 37 paralogous tetraspanin genes. Fungal proteins encoded by BcPLS1, ClPLS1, and NcPLS1 display all the structural hallmarks of tetraspanins (predicted topology with four transmembrane domains, extra- and intracellular loops; conserved cysteine-based patterns in second extracellular loop). Phylogenetic analysis suggests that these genes define a new family of orthologous genes encoding fungal-specific tetraspanins.


Assuntos
Proteínas Fúngicas/química , Fungos/metabolismo , Proteínas de Membrana/química , Proteínas de Membrana/classificação , Proteínas de Membrana/genética , Sequência de Aminoácidos , Southern Blotting , Botrytis/metabolismo , Clonagem Molecular , DNA Complementar/metabolismo , Éxons , Etiquetas de Sequências Expressas , Proteínas Fúngicas/classificação , Proteínas Fúngicas/genética , Íntrons , Magnaporthe/metabolismo , Dados de Sequência Molecular , Neurospora crassa/metabolismo , Filogenia , Reação em Cadeia da Polimerase , Estrutura Terciária de Proteína , Homologia de Sequência de Aminoácidos , Software
2.
Proc Natl Acad Sci U S A ; 98(12): 6963-8, 2001 Jun 05.
Artigo em Inglês | MEDLINE | ID: mdl-11391010

RESUMO

We describe in this study punchless, a nonpathogenic mutant from the rice blast fungus M. grisea, obtained by plasmid-mediated insertional mutagenesis. As do most fungal plant pathogens, M. grisea differentiates an infection structure specialized for host penetration called the appressorium. We show that punchless differentiates appressoria that fail to breach either the leaf epidermis or artificial membranes such as cellophane. Cytological analysis of punchless appressoria shows that they have a cellular structure, turgor, and glycogen content similar to those of wild type before penetration, but that they are unable to differentiate penetration pegs. The inactivated gene, PLS1, encodes a putative integral membrane protein of 225 aa (Pls1p). A functional Pls1p-green fluorescent protein fusion protein was detected only in appressoria and was localized in plasma membranes and vacuoles. Pls1p is structurally related to the tetraspanin family. In animals, these proteins are components of membrane signaling complexes controlling cell differentiation, motility, and adhesion. We conclude that PLS1 controls an appressorial function essential for the penetration of the fungus into host leaves.


Assuntos
Proteínas Fúngicas/genética , Genes Fúngicos/fisiologia , Magnaporthe/genética , Proteínas de Membrana/genética , Oryza/microbiologia , Sequência de Bases , Magnaporthe/patogenicidade , Dados de Sequência Molecular , Mutação
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