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Overexpression of the AP2/EREBP transcription factor OPBP1 enhances disease resistance and salt tolerance in tobacco.

Identifieur interne : 002289 ( Main/Exploration ); précédent : 002288; suivant : 002290

Overexpression of the AP2/EREBP transcription factor OPBP1 enhances disease resistance and salt tolerance in tobacco.

Auteurs : Ze-Jian Guo [République populaire de Chine] ; Xu-Jun Chen ; Xue-Long Wu ; Jian-Qun Ling ; Ping Xu

Source :

RBID : pubmed:15604704

Descripteurs français

English descriptors

Abstract

Osmotin promoter binding protein 1 (OPBP1), an AP2/EREBP-like transcription factor of tobacco (Nicotiana tabacum), was isolated using a yeast one-hybrid system. RNA gel blot analysis indicated that expression of the OPBP1 gene was induced by elicitor cryptogein, NaCl, ethephon, methyl jasmonate, as well as cycloheximide. Transient expression analysis using an OPBP1-eGFP fusion gene in onion epidermal cells revealed that the OPBP1 protein was targeted to the nuclear. Further, electrophoretic mobility shift assays demonstrated that the recombinant OPBP1 protein could bind to an oligonucleotide containing the GCC-box cis element. Transgenic tobacco plants with an over expression of the OPBP1 gene accumulated high levels of PR-1a and PR-5d genes and exhibited enhanced resistance to infection by Pseudomonas syringae pv tabaci and Phytophthora parasitica var nicotianae pathogens. They also exhibited increased tolerance to salt stress. These results suggest that OPBP1 might be a transcriptional regulator capable of regulating expression in sets of stress-related genes.

DOI: 10.1007/s11103-004-1521-3
PubMed: 15604704


Affiliations:


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Le document en format XML

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<term>Algal Proteins (pharmacology)</term>
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<term>Cycloheximide (pharmacology)</term>
<term>Cyclopentanes (pharmacology)</term>
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<term>Green Fluorescent Proteins (metabolism)</term>
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<div type="abstract" xml:lang="en">Osmotin promoter binding protein 1 (OPBP1), an AP2/EREBP-like transcription factor of tobacco (Nicotiana tabacum), was isolated using a yeast one-hybrid system. RNA gel blot analysis indicated that expression of the OPBP1 gene was induced by elicitor cryptogein, NaCl, ethephon, methyl jasmonate, as well as cycloheximide. Transient expression analysis using an OPBP1-eGFP fusion gene in onion epidermal cells revealed that the OPBP1 protein was targeted to the nuclear. Further, electrophoretic mobility shift assays demonstrated that the recombinant OPBP1 protein could bind to an oligonucleotide containing the GCC-box cis element. Transgenic tobacco plants with an over expression of the OPBP1 gene accumulated high levels of PR-1a and PR-5d genes and exhibited enhanced resistance to infection by Pseudomonas syringae pv tabaci and Phytophthora parasitica var nicotianae pathogens. They also exhibited increased tolerance to salt stress. These results suggest that OPBP1 might be a transcriptional regulator capable of regulating expression in sets of stress-related genes.</div>
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<AbstractText>Osmotin promoter binding protein 1 (OPBP1), an AP2/EREBP-like transcription factor of tobacco (Nicotiana tabacum), was isolated using a yeast one-hybrid system. RNA gel blot analysis indicated that expression of the OPBP1 gene was induced by elicitor cryptogein, NaCl, ethephon, methyl jasmonate, as well as cycloheximide. Transient expression analysis using an OPBP1-eGFP fusion gene in onion epidermal cells revealed that the OPBP1 protein was targeted to the nuclear. Further, electrophoretic mobility shift assays demonstrated that the recombinant OPBP1 protein could bind to an oligonucleotide containing the GCC-box cis element. Transgenic tobacco plants with an over expression of the OPBP1 gene accumulated high levels of PR-1a and PR-5d genes and exhibited enhanced resistance to infection by Pseudomonas syringae pv tabaci and Phytophthora parasitica var nicotianae pathogens. They also exhibited increased tolerance to salt stress. These results suggest that OPBP1 might be a transcriptional regulator capable of regulating expression in sets of stress-related genes.</AbstractText>
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