Host plant shifts affect a major defense enzyme in Chrysomela lapponica.
Identifieur interne : 001577 ( Main/Curation ); précédent : 001576; suivant : 001578Host plant shifts affect a major defense enzyme in Chrysomela lapponica.
Auteurs : Roy Kirsch [Allemagne] ; Heiko Vogel ; Alexander Muck ; Kathrin Reichwald ; Jacques M. Pasteels ; Wilhelm BolandSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2011.
Descripteurs français
- KwdFr :
- Adaptation physiologique (physiologie), Alcohol oxidoreductases (biosynthèse), Alcohol oxidoreductases (génétique), Alcools benzyliques (métabolisme), Animaux (MeSH), Betula (MeSH), Coléoptères (enzymologie), Coléoptères (génétique), Comportement alimentaire (physiologie), Données de séquences moléculaires (MeSH), Feuilles de plante (MeSH), Glucosides (métabolisme), Protéines d'insecte (biosynthèse), Protéines d'insecte (génétique), Régulation de l'expression des gènes codant pour des enzymes (physiologie), Salix (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- biosynthèse : Alcohol oxidoreductases, Protéines d'insecte.
- enzymologie : Coléoptères.
- génétique : Alcohol oxidoreductases, Coléoptères, Protéines d'insecte.
- métabolisme : Alcools benzyliques, Glucosides.
- physiologie : Adaptation physiologique, Comportement alimentaire, Régulation de l'expression des gènes codant pour des enzymes.
- Animaux, Betula, Données de séquences moléculaires, Feuilles de plante, Salix, Séquence nucléotidique.
English descriptors
- KwdEn :
- Adaptation, Physiological (physiology), Alcohol Oxidoreductases (biosynthesis), Alcohol Oxidoreductases (genetics), Animals (MeSH), Base Sequence (MeSH), Benzyl Alcohols (metabolism), Betula (MeSH), Coleoptera (enzymology), Coleoptera (genetics), Feeding Behavior (physiology), Gene Expression Regulation, Enzymologic (physiology), Glucosides (metabolism), Insect Proteins (biosynthesis), Insect Proteins (genetics), Molecular Sequence Data (MeSH), Plant Leaves (MeSH), Salix (MeSH).
- MESH :
- chemical , biosynthesis : Alcohol Oxidoreductases, Insect Proteins.
- chemical , genetics : Alcohol Oxidoreductases, Insect Proteins.
- chemical , metabolism : Benzyl Alcohols, Glucosides.
- enzymology : Coleoptera.
- genetics : Coleoptera.
- physiology : Adaptation, Physiological, Feeding Behavior, Gene Expression Regulation, Enzymologic.
- Animals, Base Sequence, Betula, Molecular Sequence Data, Plant Leaves, Salix.
Abstract
Chrysomelid leaf beetles use chemical defenses to overcome predatory attack and microbial infestation. Larvae of Chrysomela lapponica that feed on willow sequester plant-derived salicin and other leaf alcohol glucosides, which are modified in their defensive glands to bioactive compounds. Salicin is converted into salicylaldehyde by a consecutive action of a β-glucosidase and salicyl alcohol oxidase (SAO). The other leaf alcohol glucosides are not oxidized, but are deglucosylated and esterified with isobutyric- and 2-methylbutyric acid. Like some other closely related Chrysomela species, certain populations of C. lapponica shift host plants from willow to salicin-free birch. The only striking difference between willow feeders and birch feeders in terms of chemical defense is the lack of salicylaldehyde formation. To clarify the impact of host plant shifts on SAO activity, we identified and compared this enzyme by cloning, expression, and functional testing in a willow-feeding and birch-feeding population of C. lapponica. Although the birch feeders still demonstrated defensive gland-specific expression, their SAO mRNA levels were 1,000-fold lower, and the SAO enzyme was nonfunctional. Obviously, the loss of catalytic function of the SAO of birch-adapted larvae is fixed at the transcriptional, translational, and enzyme levels, thus avoiding costly expression of a highly abundant protein that is not required in the birch feeders.
DOI: 10.1073/pnas.1013846108
PubMed: 21383196
PubMed Central: PMC3064323
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Pasteels</name></author><author><name sortKey="Boland, Wilhelm" sort="Boland, Wilhelm" uniqKey="Boland W" first="Wilhelm" last="Boland">Wilhelm Boland</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adaptation, Physiological (physiology)</term><term>Alcohol Oxidoreductases (biosynthesis)</term><term>Alcohol Oxidoreductases (genetics)</term><term>Animals (MeSH)</term><term>Base Sequence (MeSH)</term><term>Benzyl Alcohols (metabolism)</term><term>Betula (MeSH)</term><term>Coleoptera (enzymology)</term><term>Coleoptera (genetics)</term><term>Feeding Behavior (physiology)</term><term>Gene Expression Regulation, Enzymologic (physiology)</term><term>Glucosides (metabolism)</term><term>Insect Proteins (biosynthesis)</term><term>Insect Proteins (genetics)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Leaves (MeSH)</term><term>Salix (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adaptation physiologique (physiologie)</term><term>Alcohol oxidoreductases (biosynthèse)</term><term>Alcohol oxidoreductases (génétique)</term><term>Alcools benzyliques (métabolisme)</term><term>Animaux (MeSH)</term><term>Betula (MeSH)</term><term>Coléoptères (enzymologie)</term><term>Coléoptères (génétique)</term><term>Comportement alimentaire (physiologie)</term><term>Données de séquences moléculaires (MeSH)</term><term>Feuilles de plante (MeSH)</term><term>Glucosides (métabolisme)</term><term>Protéines d'insecte (biosynthèse)</term><term>Protéines d'insecte (génétique)</term><term>Régulation de l'expression des gènes codant pour des enzymes (physiologie)</term><term>Salix (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Insect Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Insect Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term><term>Glucosides</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Protéines d'insecte</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Coléoptères</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Coleoptera</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coleoptera</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Coléoptères</term><term>Protéines d'insecte</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcools benzyliques</term><term>Glucosides</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Adaptation physiologique</term><term>Comportement alimentaire</term><term>Régulation de l'expression des gènes codant pour des enzymes</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Adaptation, Physiological</term><term>Feeding Behavior</term><term>Gene Expression Regulation, Enzymologic</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Base Sequence</term><term>Betula</term><term>Molecular Sequence Data</term><term>Plant Leaves</term><term>Salix</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Betula</term><term>Données de séquences moléculaires</term><term>Feuilles de plante</term><term>Salix</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Chrysomelid leaf beetles use chemical defenses to overcome predatory attack and microbial infestation. Larvae of Chrysomela lapponica that feed on willow sequester plant-derived salicin and other leaf alcohol glucosides, which are modified in their defensive glands to bioactive compounds. Salicin is converted into salicylaldehyde by a consecutive action of a β-glucosidase and salicyl alcohol oxidase (SAO). The other leaf alcohol glucosides are not oxidized, but are deglucosylated and esterified with isobutyric- and 2-methylbutyric acid. Like some other closely related Chrysomela species, certain populations of C. lapponica shift host plants from willow to salicin-free birch. The only striking difference between willow feeders and birch feeders in terms of chemical defense is the lack of salicylaldehyde formation. To clarify the impact of host plant shifts on SAO activity, we identified and compared this enzyme by cloning, expression, and functional testing in a willow-feeding and birch-feeding population of C. lapponica. Although the birch feeders still demonstrated defensive gland-specific expression, their SAO mRNA levels were 1,000-fold lower, and the SAO enzyme was nonfunctional. Obviously, the loss of catalytic function of the SAO of birch-adapted larvae is fixed at the transcriptional, translational, and enzyme levels, thus avoiding costly expression of a highly abundant protein that is not required in the birch feeders.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21383196</PMID><DateCompleted><Year>2011</Year><Month>05</Month><Day>26</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>108</Volume><Issue>12</Issue><PubDate><Year>2011</Year><Month>Mar</Month><Day>22</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Host plant shifts affect a major defense enzyme in Chrysomela lapponica.</ArticleTitle><Pagination><MedlinePgn>4897-901</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1013846108</ELocationID><Abstract><AbstractText>Chrysomelid leaf beetles use chemical defenses to overcome predatory attack and microbial infestation. Larvae of Chrysomela lapponica that feed on willow sequester plant-derived salicin and other leaf alcohol glucosides, which are modified in their defensive glands to bioactive compounds. Salicin is converted into salicylaldehyde by a consecutive action of a β-glucosidase and salicyl alcohol oxidase (SAO). The other leaf alcohol glucosides are not oxidized, but are deglucosylated and esterified with isobutyric- and 2-methylbutyric acid. Like some other closely related Chrysomela species, certain populations of C. lapponica shift host plants from willow to salicin-free birch. The only striking difference between willow feeders and birch feeders in terms of chemical defense is the lack of salicylaldehyde formation. To clarify the impact of host plant shifts on SAO activity, we identified and compared this enzyme by cloning, expression, and functional testing in a willow-feeding and birch-feeding population of C. lapponica. Although the birch feeders still demonstrated defensive gland-specific expression, their SAO mRNA levels were 1,000-fold lower, and the SAO enzyme was nonfunctional. Obviously, the loss of catalytic function of the SAO of birch-adapted larvae is fixed at the transcriptional, translational, and enzyme levels, thus avoiding costly expression of a highly abundant protein that is not required in the birch feeders.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kirsch</LastName><ForeName>Roy</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Max Planck Institute for Chemical Ecology, 07745 Jena, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vogel</LastName><ForeName>Heiko</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Muck</LastName><ForeName>Alexander</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Reichwald</LastName><ForeName>Kathrin</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Pasteels</LastName><ForeName>Jacques M</ForeName><Initials>JM</Initials></Author><Author 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