ThaumatinV1, Main, Exploration, bibRecord, 000365

Purification, characterization, and molecular gene cloning of an antifungal protein from Ginkgo biloba seeds.

Identifieur interne : 000365 ( Main/Exploration ); précédent : 000364; suivant : 000366

Purification, characterization, and molecular gene cloning of an antifungal protein from Ginkgo biloba seeds.

Auteurs : Yoriko Sawano [Japon] ; Takuya Miyakawa ; Hiroshi Yamazaki ; Masaru Tanokura ; Ken-Ichi Hatano

Source :

Biological chemistry [ 1431-6730 ] ; 2007.

RBID : pubmed:17338634

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Antifungal Agents (chemistry), Antifungal Agents (isolation & purification), Antimicrobial Cationic Peptides (genetics), Antimicrobial Cationic Peptides (isolation & purification), Base Sequence (MeSH), Cloning, Molecular (MeSH), DNA, Complementary (analysis), Disulfides (chemistry), Ginkgo biloba (chemistry), Molecular Sequence Data (MeSH), Protease Inhibitors (chemistry), Protease Inhibitors (isolation & purification), Seeds (chemistry), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH).
MESH :
- chemical , analysis : DNA, Complementary.
- chemical , chemistry : Antifungal Agents, Disulfides, Protease Inhibitors.
- chemical , genetics : Antimicrobial Cationic Peptides.
- chemical , isolation & purification : Antifungal Agents, Antimicrobial Cationic Peptides, Protease Inhibitors.
- chemistry : Ginkgo biloba, Seeds.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Molecular Sequence Data, Sequence Alignment, Sequence Homology, Amino Acid.

Abstract

A novel basic protein with antifungal activity was isolated from the seeds of Ginkgo biloba and purified to homogeneity. The protein inhibited the growth of some fungi (Fusarium oxysporum, Trichoderma reesei, and Candida albicans) but did not exhibit antibacterial action against Escherichia coli. Furthermore, this protein showed weak inhibitory activity against the aspartic protease pepsin. To design primers for gene amplification, the NH(2)-terminal and partial internal amino acid sequences were determined using peptides obtained from a tryptic digest of the oxidized protein. The full-length cDNA of the antifungal protein was cloned and sequenced by RT-PCR and rapid amplification of cDNA ends (RACE). The cDNA contained a 402-bp open reading frame encoding a 134-aa protein with a potential signal peptide (26 residues), suggesting that this protein is synthesized as a preprotein and secreted outside the cells. The antifungal protein shows approximately 85% identity with embryo-abundant proteins from Picea abies and Picea glauca at the amino acid level; however, there is no homology between this protein and other plant antifungal proteins, such as defensin, and cyclophilin-, miraculin- and thaumatin-like proteins.

DOI: 10.1515/BC.2007.030
PubMed: 17338634

Affiliations:

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Le document en format XML

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<author><name sortKey="Sawano, Yoriko" sort="Sawano, Yoriko" uniqKey="Sawano Y" first="Yoriko" last="Sawano">Yoriko Sawano</name>
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<wicri:regionArea>Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657</wicri:regionArea>
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<author><name sortKey="Miyakawa, Takuya" sort="Miyakawa, Takuya" uniqKey="Miyakawa T" first="Takuya" last="Miyakawa">Takuya Miyakawa</name>
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<author><name sortKey="Yamazaki, Hiroshi" sort="Yamazaki, Hiroshi" uniqKey="Yamazaki H" first="Hiroshi" last="Yamazaki">Hiroshi Yamazaki</name>
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<author><name sortKey="Tanokura, Masaru" sort="Tanokura, Masaru" uniqKey="Tanokura M" first="Masaru" last="Tanokura">Masaru Tanokura</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Antifungal Agents (chemistry)</term>
<term>Antifungal Agents (isolation & purification)</term>
<term>Antimicrobial Cationic Peptides (genetics)</term>
<term>Antimicrobial Cationic Peptides (isolation & purification)</term>
<term>Base Sequence (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>DNA, Complementary (analysis)</term>
<term>Disulfides (chemistry)</term>
<term>Ginkgo biloba (chemistry)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Protease Inhibitors (chemistry)</term>
<term>Protease Inhibitors (isolation & purification)</term>
<term>Seeds (chemistry)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (analyse)</term>
<term>Alignement de séquences (MeSH)</term>
<term>Antifongiques (composition chimique)</term>
<term>Antifongiques (isolement et purification)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Disulfures (composition chimique)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Ginkgo biloba (composition chimique)</term>
<term>Graines (composition chimique)</term>
<term>Inhibiteurs de protéases (composition chimique)</term>
<term>Inhibiteurs de protéases (isolement et purification)</term>
<term>Peptides antimicrobiens cationiques (génétique)</term>
<term>Peptides antimicrobiens cationiques (isolement et purification)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>DNA, Complementary</term>
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<term>Disulfides</term>
<term>Protease Inhibitors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antimicrobial Cationic Peptides</term>
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<term>Antimicrobial Cationic Peptides</term>
<term>Protease Inhibitors</term>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>ADN complémentaire</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Ginkgo biloba</term>
<term>Seeds</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Antifongiques</term>
<term>Disulfures</term>
<term>Ginkgo biloba</term>
<term>Graines</term>
<term>Inhibiteurs de protéases</term>
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<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Antifongiques</term>
<term>Inhibiteurs de protéases</term>
<term>Peptides antimicrobiens cationiques</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Cloning, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Sequence Alignment</term>
<term>Sequence Homology, Amino Acid</term>
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<term>Clonage moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">A novel basic protein with antifungal activity was isolated from the seeds of Ginkgo biloba and purified to homogeneity. The protein inhibited the growth of some fungi (Fusarium oxysporum, Trichoderma reesei, and Candida albicans) but did not exhibit antibacterial action against Escherichia coli. Furthermore, this protein showed weak inhibitory activity against the aspartic protease pepsin. To design primers for gene amplification, the NH(2)-terminal and partial internal amino acid sequences were determined using peptides obtained from a tryptic digest of the oxidized protein. The full-length cDNA of the antifungal protein was cloned and sequenced by RT-PCR and rapid amplification of cDNA ends (RACE). The cDNA contained a 402-bp open reading frame encoding a 134-aa protein with a potential signal peptide (26 residues), suggesting that this protein is synthesized as a preprotein and secreted outside the cells. The antifungal protein shows approximately 85% identity with embryo-abundant proteins from Picea abies and Picea glauca at the amino acid level; however, there is no homology between this protein and other plant antifungal proteins, such as defensin, and cyclophilin-, miraculin- and thaumatin-like proteins.</div>
</front>
</TEI>
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<DateCompleted><Year>2007</Year>
<Month>04</Month>
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<DateRevised><Year>2007</Year>
<Month>03</Month>
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<ArticleTitle>Purification, characterization, and molecular gene cloning of an antifungal protein from Ginkgo biloba seeds.</ArticleTitle>
<Pagination><MedlinePgn>273-80</MedlinePgn>
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<Abstract><AbstractText>A novel basic protein with antifungal activity was isolated from the seeds of Ginkgo biloba and purified to homogeneity. The protein inhibited the growth of some fungi (Fusarium oxysporum, Trichoderma reesei, and Candida albicans) but did not exhibit antibacterial action against Escherichia coli. Furthermore, this protein showed weak inhibitory activity against the aspartic protease pepsin. To design primers for gene amplification, the NH(2)-terminal and partial internal amino acid sequences were determined using peptides obtained from a tryptic digest of the oxidized protein. The full-length cDNA of the antifungal protein was cloned and sequenced by RT-PCR and rapid amplification of cDNA ends (RACE). The cDNA contained a 402-bp open reading frame encoding a 134-aa protein with a potential signal peptide (26 residues), suggesting that this protein is synthesized as a preprotein and secreted outside the cells. The antifungal protein shows approximately 85% identity with embryo-abundant proteins from Picea abies and Picea glauca at the amino acid level; however, there is no homology between this protein and other plant antifungal proteins, such as defensin, and cyclophilin-, miraculin- and thaumatin-like proteins.</AbstractText>
</Abstract>
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<ForeName>Yoriko</ForeName>
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<MeshHeading><DescriptorName UI="D012639" MajorTopicYN="N">Seeds</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName>
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<affiliations><list><country><li>Japon</li>
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<tree><noCountry><name sortKey="Hatano, Ken Ichi" sort="Hatano, Ken Ichi" uniqKey="Hatano K" first="Ken-Ichi" last="Hatano">Ken-Ichi Hatano</name>
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<name sortKey="Tanokura, Masaru" sort="Tanokura, Masaru" uniqKey="Tanokura M" first="Masaru" last="Tanokura">Masaru Tanokura</name>
<name sortKey="Yamazaki, Hiroshi" sort="Yamazaki, Hiroshi" uniqKey="Yamazaki H" first="Hiroshi" last="Yamazaki">Hiroshi Yamazaki</name>
</noCountry>
<country name="Japon"><region name="Région de Kantō"><name sortKey="Sawano, Yoriko" sort="Sawano, Yoriko" uniqKey="Sawano Y" first="Yoriko" last="Sawano">Yoriko Sawano</name>
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Purification, characterization, and molecular gene cloning of an antifungal protein from Ginkgo biloba seeds.

Purification, characterization, and molecular gene cloning of an antifungal protein from Ginkgo biloba seeds.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki