Full TGIF Record # 79889
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Web URL(s):https://turf.rutgers.edu/research/abstracts/symposium2002.pdf#page=48
    Last checked: 02/06/2017
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Publication Type:
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Report
Content Type:Abstract or Summary only
Author(s):Moy, Melinda; Li, Huaijun Mike; White, James F. Jr.; Belanger, Faith C.
Author Affiliation:Department of Plant Biology and Pathology, Rutgers University
Title:Glucanase expression by Clavicipitaceous endophytes in their host plants
Section:Poster presentations
Other records with the "Poster presentations" Section
Meeting Info.:Cook College, Rutgers, NJ: January 10-11, 2002
Source:Proceedings of the Eleventh Annual Rutgers TurfgrassSymposium. 2002, p. 47.
Publishing Information:New Brunswick, NJ: Center for Turfgrass Science, Cook College, Rutgers, The State University of New Jersey
# of Pages:1
Keywords:TIC Keywords: Cool season turfgrasses; Disease resistance; Endophytes; Evaluations; Gene expression; Glucanase; Hosts of plant pests
Abstract/Contents:"Some cool season grasses infected with Clavicipitaceous endophytes are known to have increased disease resistance when compared to uninfected grasses. To elucidate what endophyte derived factors might play a role in this observed disease resistance, we are attempting to clone and characterize products, such as cell well degrading enzymes, that are secreted into the apoplastic space of endophyte infected grasses. Peptide sequencing of an apoplastic protein isolated from Neotyphodium sp. infected Poa ampla leaf sheaths revealed the presence of a glucanase. Degenerate oligonucleotides were used to amplify a fragment from a cDNA library constructed from endophyte-infected leaf sheaths. The PCR clone was used to screen the cDNA library and a full-length clone was obtained. The deduced amino acid sequence of the clone was 74% identical to an endo-Β -1,6-glucanase from the mycoparasitic fungus Trichoderma harzianum (Lora et al., 1995). No other homologous sequences are in the database. Northern blot analysis demonstrated that several other endophyte-infected grasses, with increased resistance to diseases such as dollar spot, also express this glucanase. Southern blot analysis revealed that there may be a single copy of this glucanase in the Neotyphodium sp. genome. We will use a yeast expression system to characterize the activity of the protein. We have constructed a genomic library of the Neotyphodium sp. in the cosmid vector pWEB and have isolated a genomic clone for the glucanase. Sequencing of the genomic clone is currently underway. Fungal cell walls contain chitin, Β -1,3-glucans, Β -1,6-glucans, and α-1,3-glucans. In T. harzianum, the homologous endo-Β -1,6-glucanase is believed to act synergistically with other hydrolytic enzymes in the mycoparasitic activity of that fungus. We are investigating the possibility that the endophytic apoplastic hydrolytic enzymes endo-Β -1,6-glucanase, endochitinase (Li et al., 2002), and proteinase (Reddy et al., 1996) may contribute to the disease resistance observed in some endophyte-infected plants."
Language:English
References:3
Note:This item is an abstract only!
ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Moy, M., White Li. H. M, Belanger J. F. Jr., and Li. H. M F. C. 2002. Glucanase expression by Clavicipitaceous endophytes in their host plants. Proc. Annu. Rutgers Turfgrass Symp. p. 47.
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Web URL(s):
https://turf.rutgers.edu/research/abstracts/symposium2002.pdf#page=48
    Last checked: 02/06/2017
    Requires: PDF Reader
    Notes: Item is within a single large file
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MSU catalog number: SB 433 .R88
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