Serveur d'exploration sur les interactions arbre microorganisme

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Cloning and characterization of pectate lyases expressed in the esophageal gland of the pine wood nematode Bursaphelenchus xylophilus.

Identifieur interne : 000274 ( Main/Exploration ); précédent : 000273; suivant : 000275

Cloning and characterization of pectate lyases expressed in the esophageal gland of the pine wood nematode Bursaphelenchus xylophilus.

Auteurs : Taisei Kikuchi [Japon] ; Hajime Shibuya ; Takuya Aikawa ; John T. Jones

Source :

RBID : pubmed:16570658

Descripteurs français

English descriptors

Abstract

Two pectate lyase genes (Bx-pel-1 and Bx-pel-2) were cloned from the pine wood nematode, Bursaphelenchus xylophilus. The deduced amino acid sequences of these pectate lyases are most similar to polysaccharide lyase family 3 proteins. Recombinant BxPEL1 showed highest activity on polygalacturonic acid and lower activity on more highly methylated pectin. Recombinant BxPEL1 demonstrated full dependency on Ca2+ for activity and optimal activity at 55 degrees C and pH 8 to 10 like other pectate lyases of polysaccharide lyase family 3. The protein sequences have predicted signal peptides at their N-termini and the genes are expressed solely in the esophageal gland cells of the nematode, indicating that the pectate lyases could be secreted into plant tissues to help feeding and migration in the tree. This study suggests that pectate lyases are widely distributed in plant-parasitic nematodes and play an important role in plant-nematode interactions.

DOI: 10.1094/MPMI-19-0280
PubMed: 16570658


Affiliations:


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Le document en format XML

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<title xml:lang="en">Cloning and characterization of pectate lyases expressed in the esophageal gland of the pine wood nematode Bursaphelenchus xylophilus.</title>
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<name sortKey="Kikuchi, Taisei" sort="Kikuchi, Taisei" uniqKey="Kikuchi T" first="Taisei" last="Kikuchi">Taisei Kikuchi</name>
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<nlm:affiliation>Forestry and Forest Products Research Institute, Tsukuba, Ibaraki 305-8687, Japan. kikuchit@affrc.go.jp</nlm:affiliation>
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<term>Amino Acid Sequence (MeSH)</term>
<term>Animals (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Enzyme Stability (MeSH)</term>
<term>Gastrointestinal Tract (enzymology)</term>
<term>Gene Expression Regulation, Enzymologic (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Nematoda (enzymology)</term>
<term>Nematoda (genetics)</term>
<term>Phylogeny (MeSH)</term>
<term>Polysaccharide-Lyases (genetics)</term>
<term>Polysaccharide-Lyases (metabolism)</term>
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<term>Animaux (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Nematoda (enzymologie)</term>
<term>Nematoda (génétique)</term>
<term>Phylogenèse (MeSH)</term>
<term>Polysaccharide-lyases (génétique)</term>
<term>Polysaccharide-lyases (métabolisme)</term>
<term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term>
<term>Stabilité enzymatique (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Tube digestif (enzymologie)</term>
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<term>Polysaccharide-Lyases</term>
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<term>Nematoda</term>
<term>Tube digestif</term>
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<term>Régulation de l'expression des gènes codant pour des enzymes</term>
<term>Stabilité enzymatique</term>
<term>Séquence d'acides aminés</term>
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<div type="abstract" xml:lang="en">Two pectate lyase genes (Bx-pel-1 and Bx-pel-2) were cloned from the pine wood nematode, Bursaphelenchus xylophilus. The deduced amino acid sequences of these pectate lyases are most similar to polysaccharide lyase family 3 proteins. Recombinant BxPEL1 showed highest activity on polygalacturonic acid and lower activity on more highly methylated pectin. Recombinant BxPEL1 demonstrated full dependency on Ca2+ for activity and optimal activity at 55 degrees C and pH 8 to 10 like other pectate lyases of polysaccharide lyase family 3. The protein sequences have predicted signal peptides at their N-termini and the genes are expressed solely in the esophageal gland cells of the nematode, indicating that the pectate lyases could be secreted into plant tissues to help feeding and migration in the tree. This study suggests that pectate lyases are widely distributed in plant-parasitic nematodes and play an important role in plant-nematode interactions.</div>
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<AbstractText>Two pectate lyase genes (Bx-pel-1 and Bx-pel-2) were cloned from the pine wood nematode, Bursaphelenchus xylophilus. The deduced amino acid sequences of these pectate lyases are most similar to polysaccharide lyase family 3 proteins. Recombinant BxPEL1 showed highest activity on polygalacturonic acid and lower activity on more highly methylated pectin. Recombinant BxPEL1 demonstrated full dependency on Ca2+ for activity and optimal activity at 55 degrees C and pH 8 to 10 like other pectate lyases of polysaccharide lyase family 3. The protein sequences have predicted signal peptides at their N-termini and the genes are expressed solely in the esophageal gland cells of the nematode, indicating that the pectate lyases could be secreted into plant tissues to help feeding and migration in the tree. This study suggests that pectate lyases are widely distributed in plant-parasitic nematodes and play an important role in plant-nematode interactions.</AbstractText>
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