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| Publication Type:
| Refereed |
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| Author(s): | Lindstorm, Jon T.;
Belanger, Faith C. |
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| Author Affiliation: | Plant Science Department, Rutgers University, New Brunswick, NJ |
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| Title: | Purification and characterization of an endophytic fungal proteinase that is abundantly expressed in the infected host grass |
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| Source: | Plant Physiology. Vol. 106, No. 1, September 1994, p. 7-16. |
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| Publishing Information: | Rockville, MD: American Society of Plant Physiologists |
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| # of Pages: | 10 |
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| Keywords: | TIC Keywords: Endophytic fungi; Poa secunda; Acremonium; Toxicity; Fungi
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| Abstract/Contents: | "A novel Acremonium typhinum proteinase that is expressed during endophytic infection of the grass Poa ampla Merr. was purified from endophyte-infected leaf sheath tissue. It is a thiolcontaining serine alkaline endoproteinase with bound carbohydrate. In the infected host tissue, this proteinase is an abundant protein localized within fungal membrane vesicles and in the plant and/or fungal cell walls. This proteinase was not expressed constitutively during fungus culture. Rather, its expression appeared to be induced by nutrient depletion. Expression of an antigenically similar proteinase was detected in five other endophyte-infected Poa species. The regulated expression of the proteinase in culture and its abundance in infected plant tissue suggest that its expression may be involved in the symbiotic interaction of the plant and the fungus." |
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| Language: | English |
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| References: | 48 |
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| Note: | Pictures, b/w
Tables
Graphs |
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| ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Lindstorm, J. T., and F. C. Belanger. 1994. Purification and characterization of an endophytic fungal proteinase that is abundantly expressed in the infected host grass. Plant Physiol. 106(1):p. 7-16. |
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