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| Web URL(s): | https://turf.rutgers.edu/research/abstracts/symposium2002.pdf#page=46
Last checked: 02/06/2017
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| Publication Type:
| Report |
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| Content Type: | Abstract or Summary only |
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| Author(s): | Li, Huaijun Mike;
Moy, Melinda;
Kobayashi, Donald Y.;
Belanger, Faith C. |
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| Author Affiliation: | Department of Plant Biology and Pathology, Rutgers University |
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| Title: | Cloning of a Neotyphodium sp. chitinase highly expressed in infected Poa ampla |
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| Section: | Poster presentations
Other records with the "Poster presentations" Section
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| Meeting Info.: | Cook College, Rutgers, NJ: January 10-11, 2002 |
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| Source: | Proceedings of the Eleventh Annual Rutgers TurfgrassSymposium. 2002, p. 45-46. |
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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: | 2 |
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| Keywords: | TIC Keywords: Chitinase; Clones; Endophytes; Genetic analysis; Neotyphodium; Poa secunda
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| Abstract/Contents: | "Endophyte-grass associations are naturally occurring mutualistic symbioses. Endophyte-infection can confer insect resistance, and in some cases disease resistance, to the infected plant. Because of these benefits, endophytes are often incorporated into turfgrass cultivars of several species. The factors that are involved in the establishment of these mutualistic interactions and the mechanisms underlying the endophyte-enhanced traits are the targets of considerable research interest. Apoplastic secreted proteins, both plant and fungal, are likely to be important components of the mutualistic interaction since they are located at the interface of the two species. We have therefore begun investigating some of the proteins secreted in culture and apoplastic proteins isolated from infected plants. Peptide sequencing of an abundant extracellular 52 kDa protein expressed in culture identified an endochitinase. Degenerate oligonucleotides were designed based on two of the peptides and used to amplify a fragment from a cDNA library constructed from endophyte-infected P. ampla 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 had 37-40% identity to other fungal chitinases, including those of several mycoparasitic and entomopathogenic fungi (Blaiseu and Lafay, 1992; Garcia et al., 1994; St. Leger et al., 1996). The clone had an open reading frame of 1377 bp, an untranslated 5' upstream sequence of 115 bp and a 3' end of 197 bp. Computer-aided protein analysis predicted there was a signal peptide of 17 amino acids and a catalytic domain of 400 amino acids. DNA gel blot analysis indicated there is a single copy of the chitinase gene in the fungal genome. RNA gel blot analysis revealed the fungal chitinase is highly expressed in infected P. ampla leaf sheaths. A 52 kDa apoplastic protein band isolated from infected leaf sheaths was subjected to peptide sequencing. The fungal chitinase was identified as a component of the band. Native activity gel analysis using the substrates 4-MU-(GlcNAc)2 and 4-MU-(GlCNAc)3 indicated the 52 kDA protein had endochitinase activity. The endochitinase has been partially purified by binding to colloidal chitin. We now have evidence for expression of fungal endochitinase, endo-ā”-1,6-glucanase (Moy et al., 2002) and proteinase (Reddy et al., 1996) within the infected plant. In the biocontrol fungus Trichoderma harzianum the homologous enzymes are believed to function synergisitically in the mycoparasitic activity of that fungus. We are investigating the hypothesis that these Neotyphodium sp. hydrolytic enzymes located in the apoplastic space of infected plants may function as a mycolytic system for the endophyte, perhaps contributing to the observed disease resistance seen in some endophytic-infected plants." |
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| Language: | English |
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| References: | 5 |
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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):
Li, H. M., M. Moy, D. Y. Kobayashi, and F. C. Belanger. 2002. Cloning of a Neotyphodium sp. chitinase highly expressed in infected Poa ampla. Proc. Annu. Rutgers Turfgrass Symp. p. 45-46. |
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| Web URL(s):
https://turf.rutgers.edu/research/abstracts/symposium2002.pdf#page=46
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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