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  Host plant shifts affect a major defense enzyme in Chrysomela lapponica

Kirsch, R., Vogel, H., Muck, A., Reichwald, K., Pasteels, J. M., & Boland, W. (2011). Host plant shifts affect a major defense enzyme in Chrysomela lapponica. Proceedings of the National Academy of Sciences of the United States of America, 108(12), 4897-4901. doi:10.1073/pnas.1013846108.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-968B-8 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0009-8A43-0
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 Urheber:
Kirsch, Roy1, Autor           
Vogel, Heiko2, 3, Autor           
Muck, Alexandr4, Autor           
Reichwald, Kathrin, Autor
Pasteels, Jacques M., Autor
Boland, Wilhelm1, Autor           
Affiliations:
1Department of Bioorganic Chemistry, Prof. Dr. W. Boland, MPI for Chemical Ecology, Max Planck Society, ou_24028              
2Department of Entomology, Prof. D. G. Heckel, MPI for Chemical Ecology, Max Planck Society, ou_421895              
3Research Group Dr. H. Vogel, Genomics, Department of Entomology, Prof. D. G. Heckel, MPI for Chemical Ecology, Max Planck Society, Jena, DE, ou_421920              
4Research Group Mass Spectrometry, MPI for Chemical Ecology, Max Planck Society, ou_421899              

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 Zusammenfassung: 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.

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 Datum: 20112011
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: Anderer: BOL507
DOI: 10.1073/pnas.1013846108
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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : Proc. Natl. Acad. Sci. U. S. A.
Genre der Quelle: Zeitschrift
 Urheber:
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Ort, Verlag, Ausgabe: National Academy of Sciences
Seiten: - Band / Heft: 108 (12) Artikelnummer: - Start- / Endseite: 4897 - 4901 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230