Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

 
 
DownloadE-Mail
  The hepta-beta-glucoside elicitor-binding proteins from legumes represent a putative receptor family

Mithöfer, A., Fliegmann, J., Neuhaus-Url, G., Schwarz, H., & Ebel, J. (2000). The hepta-beta-glucoside elicitor-binding proteins from legumes represent a putative receptor family. Biological Chemistry, 381(8), 705-713. doi:10.1515/BC.2000.091.

Item is

Basisdaten

einblenden: ausblenden:
Genre: Zeitschriftenartikel

Dateien

einblenden: Dateien
ausblenden: Dateien
:
EXT059.pdf (Verlagsversion), 674KB
 
Datei-Permalink:
-
Name:
EXT059.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Eingeschränkt (Max Planck Institute for Chemical Ecology, MJCO; )
MIME-Typ / Prüfsumme:
application/pdf
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Mithöfer, Axel1, Autor           
Fliegmann, J., Autor
Neuhaus-Url, G., Autor
Schwarz, H., Autor
Ebel, J., Autor
Affiliations:
1External Organizations, ou_persistent22              

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: The ability of legumes to recognize and respond to beta-glucan elicitors by synthesizing phytoalexins is consistent with the existence of a membrane-bound beta-glucan-binding site. Related proteins of approximately 75 kDa and the corresponding mRNAs were detected in various species of legumes which respond to beta-glucans. The cDNAs for the beta-glucan-binding proteins of bean and soybean were cloned. The deduced 75-kDa proteins are predominantly hydrophilic and constitute a unique class of glucan-binding proteins with no currently recognizable functional domains. Heterologous expression of the soybean beta-glucan-binding protein in tomato cells resulted in the generation of a high-affinity binding site for the elicitor-active hepta-beta-glucoside conjugate (Kd = 4.5 nM). Ligand competition experiments with the recombinant binding sites demonstrated similar ligand specificities when compared with soybean. In both soybean and transgenic tomato, membrane-bound, active forms of the glucan-binding proteins coexist with immunologically detectable, soluble but inactive forms of the proteins. Reconstitution of a soluble protein fraction into lipid vesicles regained beta-glucoside-binding activity but with lower affinity (Kd = 130 nM). We conclude that the beta-glucan elicitor receptors of legumes are composed of the 75 kDa glucan-binding proteins as the critical components for ligand-recognition, and of an as yet unknown membrane anchor constituting the plasma membrane-associated receptor complex.

Details

einblenden:
ausblenden:
Sprache(n):
 Datum: 2000
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: Anderer: EXT059
DOI: 10.1515/BC.2000.091
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Biological Chemistry
  Andere : Biological Chemistry Hoppe-Seyler (Berlin)
  Kurztitel : Biol Chem Hoppe Seyler
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Berlin : W. de Gruyter
Seiten: - Band / Heft: 381 (8) Artikelnummer: - Start- / Endseite: 705 - 713 Identifikator: ISSN: 1431-6730
CoNE: https://pure.mpg.de/cone/journals/resource/954927622123