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

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_name

Plant Mol Biol

journal_title

Plant molecular biology

authors

Koo JC,Chun HJ,Park HC,Kim MC,Koo YD,Koo SC,Ok HM,Park SJ,Lee SH,Yun DJ,Lim CO,Bahk JD,Lee SY,Cho MJ

doi

10.1023/a:1019864222515

subject

Has Abstract

pub_date

2002-10-01 00:00:00

pages

441-52

issue

3

eissn

0167-4412

issn

1573-5028

journal_volume

50

pub_type

杂志文章

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