Mutualistic fungal endophytes express a proteinase that is homologous to proteases suspected to be important in fungal pathogenicity.
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Journal: 1996/October - Plant Physiology
ISSN: 0032-0889
PUBMED: 8756501
Abstract:
Many cultivated and wild grass species are hosts to mutualistic fungal endophytes. These associations are ecologically and agronomically significant, yet little is known regarding the physiological aspects of the interaction. In the Poa ampla/Acremonium typhinum interaction, a fungal serine proteinase, At1, is surprisingly abundant and may constitute 1 to 2% of the total leaf-sheath protein. Sequence analysis of cDNA and genomic clones indicates that proteinase At1 is a member of the eukaryotic subtilisin-like protease family. It is homologous to proteases suspected to be virulence factors in fungal pathogens of insects, nematodes, and other fungi. Gel blot analysis of RNA extracted from infected leaf-sheath tissue indicates that the proteinase At1 transcript level is extremely high. RNA gel blots and immunoblots of purified enzymes indicate that similar proteinases are produced by Epichloë festucae and Acremonium lolii, the fungal endophytes infecting Festuca rubra subsp. rubra and Lolium perenne, respectively. Fungal expression of proteinase At1-like enzymes may be a general feature of endophyte infection.
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Plant Physiol 111(4): 1209-1218
PMID: 8756501

Mutualistic fungal endophytes express a proteinase that is homologous to proteases suspected to be important in fungal pathogenicity.

Abstract

Many cultivated and wild grass species are hosts to mutualistic fungal endophytes. These associations are ecologically and agronomically significant, yet little is known regarding the physiological aspects of the interaction. In the Poa ampla/Acremonium typhinum interaction, a fungal serine proteinase, At1, is surprisingly abundant and may constitute 1 to 2% of the total leaf-sheath protein. Sequence analysis of cDNA and genomic clones indicates that proteinase At1 is a member of the eukaryotic subtilisin-like protease family. It is homologous to proteases suspected to be virulence factors in fungal pathogens of insects, nematodes, and other fungi. Gel blot analysis of RNA extracted from infected leaf-sheath tissue indicates that the proteinase At1 transcript level is extremely high. RNA gel blots and immunoblots of purified enzymes indicate that similar proteinases are produced by Epichloë festucae and Acremonium lolii, the fungal endophytes infecting Festuca rubra subsp. rubra and Lolium perenne, respectively. Fungal expression of proteinase At1-like enzymes may be a general feature of endophyte infection.

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Department of Plant Pathology, Rutgers University, New Brunswick, New Jersey 08903, USA.
Department of Plant Pathology, Rutgers University, New Brunswick, New Jersey 08903, USA.
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Abstract

Many cultivated and wild grass species are hosts to mutualistic fungal endophytes. These associations are ecologically and agronomically significant, yet little is known regarding the physiological aspects of the interaction. In the Poa ampla/Acremonium typhinum interaction, a fungal serine proteinase, At1, is surprisingly abundant and may constitute 1 to 2% of the total leaf-sheath protein. Sequence analysis of cDNA and genomic clones indicates that proteinase At1 is a member of the eukaryotic subtilisin-like protease family. It is homologous to proteases suspected to be virulence factors in fungal pathogens of insects, nematodes, and other fungi. Gel blot analysis of RNA extracted from infected leaf-sheath tissue indicates that the proteinase At1 transcript level is extremely high. RNA gel blots and immunoblots of purified enzymes indicate that similar proteinases are produced by Epichloë festucae and Acremonium lolii, the fungal endophytes infecting Festuca rubra subsp. rubra and Lolium perenne, respectively. Fungal expression of proteinase At1-like enzymes may be a general feature of endophyte infection.

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