Título

Hetero- and homodimerization of Arabidopsis thaliana arginine decarboxylase AtADC1 and AtADC2

Autor

Israel Maruri López

JUAN FRANCISCO JIMENEZ BREMONT

Nivel de Acceso

Acceso Abierto

Identificador alterno

doi: https://doi.org/10.1016/j.bbrc.2017.01.083

Resumen o descripción

"The arginine decarboxylase enzyme (ADC) carries out the production of agmatine from arginine, which is the precursor of the first polyamine (PA) known as putrescine; subsequently, putrescine is turned into the higher PAs, spermidine and spermine. In Arabidopsis thaliana PA production occurs only from arginine and this step is initiated by two ADC paralogues, AtADC1 and AtADC2. PA production is essential for A. thaliana life cycle. Here, we analyzed the sub-cellular localization of AtADC1 and AtADC2 enzymes through GFP translational fusions. Our data revealed that the A. thaliana arginine decarboxylase enzymes exhibit a dual sub-cellular localization both in the cytosol and chloroplast. Moreover, we examined the protein dimer assembly using a Bimolecular Fluorescence Complementation (BiFC) approach, which showed that AtADC1 and AtADC2 proteins were able to form homodimers in the cytosol and chloroplast. Interestingly, we found the formation of AtADC1/AtADC2 heterodimers with similar sub-cellular localization than homodimers. This study reveals that both ADC proteins are located in the same cell compartments, and they are able to form protein interaction complexes with each other."

Editor

Elsevier

Fecha de publicación

2017

Tipo de publicación

Artículo

Versión de la publicación

Versión aceptada

Formato

application/pdf

Sugerencia de citación

Israel Maruri-López, Juan F. Jiménez-Bremont, Hetero- and homodimerization of Arabidopsis thaliana arginine decarboxylase AtADC1 and AtADC2, Biochemical and Biophysical Research Communications, Volume 484, Issue 3, 2017, Pages 508-513.

Repositorio Orígen

Repositorio IPICYT

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