A Polyamine Metabolon Involving Aminopropyl Transferase Complexes in Arabidopsis (original) (raw)

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Mireia Panicot ,

aUnitat de Fisiologia Vegetal, Facultat de Farmàcia, Universitat de Barcelona, Diagonal 643, 08028-Barcelona, Spain

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Eugenio G. Minguet ,

bInstituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia–Consejo Superior de Investigaciones Científicas, Avda de los Naranjos s/n, 46022 Valencia, Spain

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Alejandro Ferrando ,

cMax-Planck-Institut für Züchtungsforschung, Carl-von-Linné-Weg 10, D-50829 Köln, Germany

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Rubén Alcázar ,

aUnitat de Fisiologia Vegetal, Facultat de Farmàcia, Universitat de Barcelona, Diagonal 643, 08028-Barcelona, Spain

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Miguel A. Blázquez ,

bInstituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia–Consejo Superior de Investigaciones Científicas, Avda de los Naranjos s/n, 46022 Valencia, Spain

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Juan Carbonell ,

bInstituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia–Consejo Superior de Investigaciones Científicas, Avda de los Naranjos s/n, 46022 Valencia, Spain

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Teresa Altabella ,

aUnitat de Fisiologia Vegetal, Facultat de Farmàcia, Universitat de Barcelona, Diagonal 643, 08028-Barcelona, Spain

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Csaba Koncz ,

cMax-Planck-Institut für Züchtungsforschung, Carl-von-Linné-Weg 10, D-50829 Köln, Germany

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Antonio F. Tiburcio

aUnitat de Fisiologia Vegetal, Facultat de Farmàcia, Universitat de Barcelona, Diagonal 643, 08028-Barcelona, Spain

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Published:

01 October 2002

Cite

Mireia Panicot, Eugenio G. Minguet, Alejandro Ferrando, Rubén Alcázar, Miguel A. Blázquez, Juan Carbonell, Teresa Altabella, Csaba Koncz, Antonio F. Tiburcio, A Polyamine Metabolon Involving Aminopropyl Transferase Complexes in Arabidopsis , The Plant Cell, Volume 14, Issue 10, October 2002, Pages 2539–2551, https://doi.org/10.1105/tpc.004077
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Abstract

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 spe_Δ_3 deficiency of spermidine synthase in yeast. However, SPMS was able to complement the spe_Δ_4 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.

© 2002 American Society of Plant Biologists

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