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
Materias
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
Recurso de información
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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