Gene Ontology annotation through association of InterPro records with GO terms
Combined Automated Annotation using Multiple IEA Methods
MPG1 Encodes a Fungal Hydrophobin Involved in Surface Interactions during Infection-Related Development of Magnaporthe grisea.
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MPG1 is required for the conidial rodlet layer and conidial hydrophobicity, and encodes a secreted 15-kD class I hydrophobin that forms detergent-insoluble complexes.
"Ultrastructural studies revealed that MPG1 directs formation of a rodlet layer on conidia composed of interwoven ~5-nm rodlets, which contributes to their surface hydrophobicity."
Four conserved intramolecular disulphide linkages are required for secretion and cell wall localization of a hydrophobin during fungal morphogenesis.
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Disulphide bonds are dispensable for MPG1 self-assembly but essential for its secretion to the cell surface.
"disulphide bridges in a hydrophobin are dispensable for aggregation, but essential for secretion"
Identification and characterization of MPG1, a gene involved in pathogenicity from the rice blast fungus Magnaporthe grisea.
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mpg1 mutants are easily wettable and have reduced appressorium formation and disease symptoms.
"Mpg1 mutants have a reduced ability to cause disease symptoms that appears to result from an impaired ability to undergo appressorium formation."
MPG1, a gene encoding a fungal hydrophobin of Magnaporthe grisea, is involved in surface recognition.
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MPG1 is required for efficient appressorium induction on host and highly hydrophobic surfaces but not on some artificial substrates; the defect is rescued in trans by wild-type cells.
"This finding suggests that Mpg1p is not specifically required for appressorium formation, but is involved in the interaction with, and recognition of, the host surface."
Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism.
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Purified MPG1 assembles into functional amyloid rodlets only at a hydrophobic:hydrophilic interface; MPG1 coatings retain cutinase 2 activity.
"We show that MPG1 self-assembly into functional amyloid rodlets is strictly limited to a hydrophobic:hydrophilic interface."
Regulation of the MPG1 hydrophobin gene in the rice blast fungus Magnaporthe grisea.
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MPG1 expression requires PMK1, NPR1 and NUT1 under starvation and is repressed via CPKA in rich medium.
"The MAP kinase-encoding gene PMK1 and the wide domain regulators of nitrogen source utilization, NPR1 and NUT1, were required for full expression of MPG1 in response to starvation stress."
Falcon (Edison Scientific) deep research report for MPG1