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  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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3D69-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3D6A-9
Genre: Journal Article

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 Creators:
Panicot, M.1, Author              
Minguet, E. G., Author
Ferrando, A.2, Author              
Alcázar, R.3, Author              
Blazquez, M. A., Author
Carbonell, J., Author
Altabella, T., Author
Koncz, C.1, Author              
Tiburcio, A. F., Author
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              

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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 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.

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Language(s): eng - English
 Dates: 2002-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 28777
ISI: 000178740100017
 Degree: -

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Title: Plant Cell
  Alternative Title : Plant Cell
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 14 (10) Sequence Number: - Start / End Page: 2539 - 2551 Identifier: ISSN: 1040-4651