Over-expression of a seed specific hevein-like antimicrobial peptide from Pharbitis nil enhances resistance to a fungal pathogen in transgenic tobacco plants

Over-expression of a seed specific hevein-like antimicrobial peptide from Pharbitis nil enhances... Two hevein-like peptides from the seed of Pharbitis nil, designated Pharbitis nil antimicrobial peptide 1 (Pn-AMP1) and Pn-AMP2, had been purified previously. Both exhibit potent in vitro antifungal activity against a broad spectrum of phytopathogenic fungi. We now report the isolation of two cDNA clones, designated pnAMP-h1 and pnAMP-h2, and the corresponding genomic clones encoding these proteins from mature seeds of P. nil. Comparison of the deduced amino acid sequence to that of the mature protein suggests that the peptides are produced as a prepropeptide consisting of an N-terminal signal peptide, the mature protein and C-terminal domains. The transcripts of the two genes are accumulated seed-specifically, and the maximum transcripts are observed in the mid-to-late stage of seed development. Constitutive over-expression of the pnAMP-h2 cDNA in transgenic tobacco under the control of the cauliflower mosaic virus 35S promoter conferred enhanced resistance against the oomycete Phytophthora parasitica, the causal agent of black shank disease. Thus the Pn-AMPs may play a role in the protection of seeds and may be useful as a novel gene source to engineer plants resistant to fungal pathogens. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Over-expression of a seed specific hevein-like antimicrobial peptide from Pharbitis nil enhances resistance to a fungal pathogen in transgenic tobacco plants

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 2002 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1019864222515
Publisher site
See Article on Publisher Site

Abstract

Two hevein-like peptides from the seed of Pharbitis nil, designated Pharbitis nil antimicrobial peptide 1 (Pn-AMP1) and Pn-AMP2, had been purified previously. Both exhibit potent in vitro antifungal activity against a broad spectrum of phytopathogenic fungi. We now report the isolation of two cDNA clones, designated pnAMP-h1 and pnAMP-h2, and the corresponding genomic clones encoding these proteins from mature seeds of P. nil. Comparison of the deduced amino acid sequence to that of the mature protein suggests that the peptides are produced as a prepropeptide consisting of an N-terminal signal peptide, the mature protein and C-terminal domains. The transcripts of the two genes are accumulated seed-specifically, and the maximum transcripts are observed in the mid-to-late stage of seed development. Constitutive over-expression of the pnAMP-h2 cDNA in transgenic tobacco under the control of the cauliflower mosaic virus 35S promoter conferred enhanced resistance against the oomycete Phytophthora parasitica, the causal agent of black shank disease. Thus the Pn-AMPs may play a role in the protection of seeds and may be useful as a novel gene source to engineer plants resistant to fungal pathogens.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 13, 2004

References

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