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Molecular cloning and characterization of a novel bi-functional α-amylase/subtilisin inhibitor from Hevea brasiliensis.

Identifieur interne : 000B74 ( Main/Exploration ); précédent : 000B73; suivant : 000B75

Molecular cloning and characterization of a novel bi-functional α-amylase/subtilisin inhibitor from Hevea brasiliensis.

Auteurs : Orawan Bunyatang [Thaïlande] ; Nion Chirapongsatonkul [Thaïlande] ; Phuwadol Bangrak [Thaïlande] ; Robert Henry [Australie] ; Nunta Churngchow [Thaïlande]

Source :

RBID : pubmed:26854410

Descripteurs français

English descriptors

Abstract

A novel cDNA encoding a bi-functional α-amylase/subtilisin inhibitor (HbASI) was isolated from rubber (Hevea brasiliensis) leaves cultivar RRIM600. The HbASI had strong homology with the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. Its putative amino acid sequence was similar to that of the α-amylase/subtilisin inhibitor from Ricinus communis (72% identity). Genomic sequencing indicated that the HbASI gene contained no introns. The messenger RNA of HbASI was detected in leaf, hypocotyl and root. The recombinant HbASI expressed extracellularly in Pichia pastoris exhibited inhibitory activity against α-amylase from Aspergillus oryzae, trypsin and subtilisin A. The HbASI gene was induced in the rubber leaves infected with a rubber tree pathogen, Phytophthora palmivora. It was also enhanced by salicylic acid (SA) treatment and mechanical wounding. In addition, the biological activity of the HbASI protein involving in the plant defence responses was also investigated. The HbASI at a concentration of 0.16 mg mL(-1) could inhibit the mycelium growth of P. palmivora. These data suggested that the HbASI protein might play a crucial role in defence against pathogen of rubber trees.

DOI: 10.1016/j.plaphy.2016.01.014
PubMed: 26854410


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<term>Cloning, Molecular (MeSH)</term>
<term>Enzyme Inhibitors (chemistry)</term>
<term>Enzyme Inhibitors (metabolism)</term>
<term>Enzyme Inhibitors (pharmacology)</term>
<term>Hevea (chemistry)</term>
<term>Hevea (genetics)</term>
<term>Hevea (metabolism)</term>
<term>Mycelium (growth & development)</term>
<term>Phytophthora (growth & development)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Plant Proteins (pharmacology)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Recombinant Proteins (pharmacology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Antienzymes (composition chimique)</term>
<term>Antienzymes (métabolisme)</term>
<term>Antienzymes (pharmacologie)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Hevea (composition chimique)</term>
<term>Hevea (génétique)</term>
<term>Hevea (métabolisme)</term>
<term>Mycelium (croissance et développement)</term>
<term>Phytophthora (croissance et développement)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Protéines recombinantes (pharmacologie)</term>
<term>Protéines végétales (composition chimique)</term>
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<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
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<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
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<term>Recombinant Proteins</term>
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<term>Enzyme Inhibitors</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
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<term>Antienzymes</term>
<term>Hevea</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
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<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr">
<term>Mycelium</term>
<term>Phytophthora</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Hevea</term>
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<keywords scheme="MESH" qualifier="growth & development" xml:lang="en">
<term>Mycelium</term>
<term>Phytophthora</term>
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<term>Protéines recombinantes</term>
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<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
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<div type="abstract" xml:lang="en">A novel cDNA encoding a bi-functional α-amylase/subtilisin inhibitor (HbASI) was isolated from rubber (Hevea brasiliensis) leaves cultivar RRIM600. The HbASI had strong homology with the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. Its putative amino acid sequence was similar to that of the α-amylase/subtilisin inhibitor from Ricinus communis (72% identity). Genomic sequencing indicated that the HbASI gene contained no introns. The messenger RNA of HbASI was detected in leaf, hypocotyl and root. The recombinant HbASI expressed extracellularly in Pichia pastoris exhibited inhibitory activity against α-amylase from Aspergillus oryzae, trypsin and subtilisin A. The HbASI gene was induced in the rubber leaves infected with a rubber tree pathogen, Phytophthora palmivora. It was also enhanced by salicylic acid (SA) treatment and mechanical wounding. In addition, the biological activity of the HbASI protein involving in the plant defence responses was also investigated. The HbASI at a concentration of 0.16 mg mL(-1) could inhibit the mycelium growth of P. palmivora. These data suggested that the HbASI protein might play a crucial role in defence against pathogen of rubber trees. </div>
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<AbstractText>A novel cDNA encoding a bi-functional α-amylase/subtilisin inhibitor (HbASI) was isolated from rubber (Hevea brasiliensis) leaves cultivar RRIM600. The HbASI had strong homology with the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. Its putative amino acid sequence was similar to that of the α-amylase/subtilisin inhibitor from Ricinus communis (72% identity). Genomic sequencing indicated that the HbASI gene contained no introns. The messenger RNA of HbASI was detected in leaf, hypocotyl and root. The recombinant HbASI expressed extracellularly in Pichia pastoris exhibited inhibitory activity against α-amylase from Aspergillus oryzae, trypsin and subtilisin A. The HbASI gene was induced in the rubber leaves infected with a rubber tree pathogen, Phytophthora palmivora. It was also enhanced by salicylic acid (SA) treatment and mechanical wounding. In addition, the biological activity of the HbASI protein involving in the plant defence responses was also investigated. The HbASI at a concentration of 0.16 mg mL(-1) could inhibit the mycelium growth of P. palmivora. These data suggested that the HbASI protein might play a crucial role in defence against pathogen of rubber trees. </AbstractText>
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<DescriptorName UI="D028482" MajorTopicYN="Y">Hevea</DescriptorName>
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<Keyword MajorTopicYN="N">Hevea brasiliensis</Keyword>
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<name sortKey="Chirapongsatonkul, Nion" sort="Chirapongsatonkul, Nion" uniqKey="Chirapongsatonkul N" first="Nion" last="Chirapongsatonkul">Nion Chirapongsatonkul</name>
<name sortKey="Churngchow, Nunta" sort="Churngchow, Nunta" uniqKey="Churngchow N" first="Nunta" last="Churngchow">Nunta Churngchow</name>
</country>
<country name="Australie">
<noRegion>
<name sortKey="Henry, Robert" sort="Henry, Robert" uniqKey="Henry R" first="Robert" last="Henry">Robert Henry</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

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   |texte=   Molecular cloning and characterization of a novel bi-functional α-amylase/subtilisin inhibitor from Hevea brasiliensis.
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