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A novel zinc-binding alcohol dehydrogenase 2 from Arachis diogoi, expressed in resistance responses against late leaf spot pathogen, induces cell death when transexpressed in tobacco
Year:
2016
Source of publication :
FEBS Open Bio
Authors :
Kumar, Dilip
;
.
Volume :
6
Co-Authors:
Kumar, D., Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India
Rampuria, S., Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India
Singh, N.K., Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India
Kirti, P.B., Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India
Facilitators :
From page:
200
To page:
210
(
Total pages:
11
)
Abstract:
A novel zinc-binding alcohol dehydrogenase 2 (AdZADH2) was significantly upregulated in a wild peanut, Arachis diogoi treated with conidia of late leaf spot (LLS) pathogen, Phaeoisariopsis personata. This upregulation was not observed in a comparative analysis of cultivated peanut, which is highly susceptible to LLS. This zinc-binding alcohol dehydrogenase possessed a Rossmann fold containing NADB domain in addition to the MDR domain present in all previously characterized plant ADH genes/proteins. Transient over-expression of AdZADH2 under an estradiol inducible promoter (XVE) resulted in hypersensitive response (HR)-like cell death in tobacco leaf. However, the same level of cell death was not observed when the domains were transiently expressed individually. Cell death observed in tobacco was associated with overexpression of cell death related proteins, antioxidative enzymes such as SOD, CAT and APX and pathogenesis-related (PR) proteins. In A. diogoi, AdZADH2 expression was significantly upregulated in response to the plant signaling hormones salicylic acid, methyl jasmonate, and sodium nitroprusside. © 2016 Federation of European Biochemical Societies.
Note:
Related Files :
Arachis diogoi
HR-like cell death
Rossmann fold containing NADB domain
Zinc-binding alcohol dehydrogenase 2
Show More
Related Content
More details
DOI :
10.1002/2211-5463.12040
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28212
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:37
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Scientific Publication
A novel zinc-binding alcohol dehydrogenase 2 from Arachis diogoi, expressed in resistance responses against late leaf spot pathogen, induces cell death when transexpressed in tobacco
6
Kumar, D., Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India
Rampuria, S., Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India
Singh, N.K., Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India
Kirti, P.B., Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India
A novel zinc-binding alcohol dehydrogenase 2 from Arachis diogoi, expressed in resistance responses against late leaf spot pathogen, induces cell death when transexpressed in tobacco
A novel zinc-binding alcohol dehydrogenase 2 (AdZADH2) was significantly upregulated in a wild peanut, Arachis diogoi treated with conidia of late leaf spot (LLS) pathogen, Phaeoisariopsis personata. This upregulation was not observed in a comparative analysis of cultivated peanut, which is highly susceptible to LLS. This zinc-binding alcohol dehydrogenase possessed a Rossmann fold containing NADB domain in addition to the MDR domain present in all previously characterized plant ADH genes/proteins. Transient over-expression of AdZADH2 under an estradiol inducible promoter (XVE) resulted in hypersensitive response (HR)-like cell death in tobacco leaf. However, the same level of cell death was not observed when the domains were transiently expressed individually. Cell death observed in tobacco was associated with overexpression of cell death related proteins, antioxidative enzymes such as SOD, CAT and APX and pathogenesis-related (PR) proteins. In A. diogoi, AdZADH2 expression was significantly upregulated in response to the plant signaling hormones salicylic acid, methyl jasmonate, and sodium nitroprusside. © 2016 Federation of European Biochemical Societies.
Scientific Publication
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