Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

 
 
DownloadE-Mail
  A polyamine metabolon involving aminopropyl transferase complexes in Arabidopsis

Panicot, M., Minguet, E. G., Ferrando, A., Alcázar, R., Blazquez, M. A., Carbonell, J., et al. (2002). A polyamine metabolon involving aminopropyl transferase complexes in Arabidopsis. Plant Cell, 14(10), 2539-2551.

Item is

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Panicot, M.1, Autor           
Minguet, E. G., Autor
Ferrando, A.2, Autor           
Alcázar, R.3, Autor           
Blazquez, M. A., Autor
Carbonell, J., Autor
Altabella, T., Autor
Koncz, C.1, Autor           
Tiburcio, A. F., Autor
Affiliations:
1Dept. of Plant Developmental Biology (George Coupland), MPI for Plant Breeding Research, Max Planck Society, ou_1113571              
2Dept. of Genetic Principles of Plant Breeding (Jozef Schell), MPI for Plant Breeding Research, Max Planck Society, ou_1113567              
3Dept. of Plant Breeding and Genetics (Maarten Koornneef), MPI for Plant Breeding Research, Max Planck Society, ou_1113569              

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: The conversion of putrescine to spermidine in the biosynthetic pathway of plant polyamines is catalyzed by two closely related spermidine synthases, SPDS1 and SPDS2, in Arabidopsis. In the yeast two-hybrid system, SPDS2 was found to interact with SPDS1 and a novel protein, SPMS (spermine synthase), which is homologous with SPDS2 and SPDS1. SPMS interacts with both SPDS1 and SPDS2 in yeast and in vitro. Unlike SPDS1 and SPDS2, SPMS failed to suppress the speDelta3 deficiency of spermidine synthase in yeast. However, SPMS was able to complement the speDelta4 spermine deficiency in yeast, indicating that SPMS is a novel spermine synthase. The SPDS and SPMS proteins showed no homodimerization but formed heterodimers in vitro. Pairwise coexpression of hemagglutinin- and c-Myc epitope-labeled proteins in Arabidopsis cells confirmed the existence of coimmunoprecipitating SPDS1-SPDS2 and SDPS2-SPMS heterodimers in vivo. The epitope-labeled SPDS and SPMS proteins copurified with protein complexes ranging in size from 650 to 750 kD. Our data demonstrate the existence of a metabolon involving at least the last two steps of polyamine biosynthesis in Arabidopsis.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2002-10
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 28777
ISI: 000178740100017
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Plant Cell
  Alternativer Titel : Plant Cell
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 14 (10) Artikelnummer: - Start- / Endseite: 2539 - 2551 Identifikator: ISSN: 1040-4651