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Genome-wide identification, expression and chromosomal location of the genes encoding chitinolytic enzymes in Zea mays
Year:
2008
Source of publication :
Molecular Genetics and Genomics
Authors :
Shoresh, Michal
;
.
Volume :
280
Co-Authors:
Shoresh, M., Department of Horticultural Sciences, Cornell University, Geneva, NY 14456, United States, Institute of Soil, Water, and Environmental Sciences, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Harman, G.E., Department of Horticultural Sciences, Cornell University, Geneva, NY 14456, United States
Facilitators :
From page:
173
To page:
185
(
Total pages:
13
)
Abstract:
Chitinolytic enzymes are important pathogenesis and stress related proteins. We identified 27 putative genes encoding endochitinases in the maize genome via in silico techniques and four exochitinases. Only seven of the endochitinases and segments of the exochitinases were heretofore known. The endochitinases included members of family 19 chitinases (classes I-IV of PR3, II of PR4) and members of family 18 chitinases (class III of PR8). Some similar enzymes were detected on adjacent regions of the same chromosome, and seem to result from duplication events. Most of the genes expressed were identified from EST libraries from plants exposed to biotic or abiotic stresses but also from libraries from tissues not exposed to stresses. We isolated proteins from seedlings of maize in the presence or absence of the symbiotic root colonizing fungus Trichoderma harzianum strain T22, and analyzed the activity of chitinolytic enzymes using an in-gel activity assay. The activity bands were identified by LC/MS/MS using the database from our in silico study. The identities of the enzymes changed depending on whether or not T22 was present. One activity band of about 95 kDa appeared to be a heterodimer between an exochitinase and any of several different endochitinases. The identity of the endochitinase component appeared to be dependent upon treatment. © 2008 Springer-Verlag.
Note:
Related Files :
chromosome mapping
fungi
Gene
gene expression
Genome
Trichoderma
Zea mays
Show More
Related Content
More details
DOI :
10.1007/s00438-008-0354-1
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
19947
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:32
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Scientific Publication
Genome-wide identification, expression and chromosomal location of the genes encoding chitinolytic enzymes in Zea mays
280
Shoresh, M., Department of Horticultural Sciences, Cornell University, Geneva, NY 14456, United States, Institute of Soil, Water, and Environmental Sciences, Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Harman, G.E., Department of Horticultural Sciences, Cornell University, Geneva, NY 14456, United States
Genome-wide identification, expression and chromosomal location of the genes encoding chitinolytic enzymes in Zea mays
Chitinolytic enzymes are important pathogenesis and stress related proteins. We identified 27 putative genes encoding endochitinases in the maize genome via in silico techniques and four exochitinases. Only seven of the endochitinases and segments of the exochitinases were heretofore known. The endochitinases included members of family 19 chitinases (classes I-IV of PR3, II of PR4) and members of family 18 chitinases (class III of PR8). Some similar enzymes were detected on adjacent regions of the same chromosome, and seem to result from duplication events. Most of the genes expressed were identified from EST libraries from plants exposed to biotic or abiotic stresses but also from libraries from tissues not exposed to stresses. We isolated proteins from seedlings of maize in the presence or absence of the symbiotic root colonizing fungus Trichoderma harzianum strain T22, and analyzed the activity of chitinolytic enzymes using an in-gel activity assay. The activity bands were identified by LC/MS/MS using the database from our in silico study. The identities of the enzymes changed depending on whether or not T22 was present. One activity band of about 95 kDa appeared to be a heterodimer between an exochitinase and any of several different endochitinases. The identity of the endochitinase component appeared to be dependent upon treatment. © 2008 Springer-Verlag.
Scientific Publication
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