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| Publication Type:
| Report |
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| Content Type: | Abstract or Summary only |
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| Author(s): | Lindstrom, Jon T.;
Sun, Suichang;
Belanger, Faith C. |
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| Author Affiliation: | Plant Science Department, Rutgers University, New Brunswick, New Jersey |
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| Title: | A novel fungal protease expressed in endophytic infection of Poa species |
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| Section: | Oral presentation
Other records with the "Oral presentation" Section
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| Meeting Info.: | Cook College, Rutgers, NJ: January 15-16, 1993 |
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| Source: | Proceedings of the Second Annual Rutgers TurfgrassSymposium. Vol. 2, 1993, p. 8. |
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| Publishing Information: | New Brunswick, NJ: Center for Turfgrass Science, Cook College, Rutgers, The State University of New Jersey |
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| # of Pages: | 1 |
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| Keywords: | TIC Keywords: Endophytes; Fungi; Physiology; Proteases; Acremonium typhinum; Poa secunda; Festuca; Lolium perenne; Symbiosis
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| Abstract/Contents: | "We are interested in the physiology of the interaction of fungal endophytes with their host turfgrass species. We have detected a novel fungal protease which may be important in the endophytic infection of Poa species. Our initial characterization of the protease has been done on the Acremonium thypinum isolate from the host grass Poa ampla. This protease is expressed in the symbiosis with its host plant, but is not expressed on long term axenic culture of the species. We have detected a similar protease activity in two other endophyte-infected Poa species. We have not detected similar protease activities in endophyte-infected tall fescues or fine fescues, both Festuca species, or in endophyte-infected ryegrass, Lolium perenne. This observation suggests that expression of this protease may be important in the symbiotic relationship of Poa species with fungal endophyes. In addition to its possible importance in the symbiosis of Acremonium endophytes with Poa species, this protease is interesting because of its unusual characteristics. The protease is highly active in conditions considered to be denaturing, i.e. 2X SDS buffer (4.6% SDS which is 160 mM). In this regard the Acremonium protease is similar to Proteinase K from the fungus Tritirachium album which is also highly active in the presence of SDS. In size and in its membrane localization, however, the Acremonium protease is distinct from Proteinase K which is a secreted Mr 18,500 protein. Based on its inhibition with PMSF but not E-64 and its requirement for a reductant the Acremonium protease appears to be a serine protease with an essential thiol group. The Acremonium protease migrated in an SDS-gelatin gel with an apparent molecular weight considerably greater than 205,000. Further characterization of the protein will be required to determine if the electrophoretic migration is an anomaly of protein modification or if it truly reflects the size of the protease. Activity was localized to a crude membrane fraction. Localization to a specific membrane system will aid in understanding the importance of the protease in the plant-fungus interaction." |
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| Language: | English |
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| References: | 0 |
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| Note: | This item is an abstract only! |
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| ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Lindstrom, J. T., F. C. Belanger, and S. Sun. 1993. A novel fungal protease expressed in endophytic infection of Poa species. Proc. Annu. Rutgers Turfgrass Symp. 2:p. 8. |
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MSU catalog number: SB 433 .R88 |
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