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Título: | Occurrence of carbon catabolite repression-regulated mechanism involved in the transport of extracellular ADP-glucose in Escherichia coli |
Autor: | Almagro, Goizeder CSIC ORCID ; Montero, Manuel CSIC ORCID; Viale, Alejandro M. CSIC; Rahimpour, Mehdi CSIC; Bahaji, Abdellatif CSIC ORCID ; Muñoz Pérez, Francisco José CSIC ORCID ; Baroja-Fernández, Edurne CSIC ORCID CVN ; Pozueta Romero, Javier CSIC ORCID | Fecha de publicación: | sep-2014 | Citación: | XXXVII Congreso de la Sociedad Española de Bioquímica y Biología Molecular (2014) | Resumen: | ADP-glucose is the precursor molecule for glycogen and starch biosynthesis in bacteria and plants, respectively. Due to the high abundance of this nucleotide-sugar in tubers and endosperms present in the normal diet of many animals, we explored the possible occurrence of an ADP-glucose transport system in the enterobacterial species Escherichia coli. To avoid artifacts resulting from the possible conversion of periplasmic ADP-glucose breakdown products into glycogen, in this work we used glglC and pgm null mutants unable to catalyze the reversible conversion of ADP-glucose into glucose-1-P, and glucose-1-P into glucose-6-phosphate, respectively. Noteworthy, these cells converted the exogenoulsy added ADP-glucose into glycogen. Uptake of ADP-glucose was confirmed by the disappearance of this nucleotide-sugar from the culture medium. ΔpgmΔptsG, ΔpgmΔptsH, ΔpgmΔptsI and ΔpgmΔcrr cells impaired in the PTS components produced glycogen from exogenously added ADP-glucose, indicating that the transport of this nucleotide-sugar is not mediated by PTS. Furthermore, ΔpgmΔcyaA and ΔpgmΔcrp cells, both impaired in the CRP-cAMP carbon catabolite repression mechanism, neither incorporated ADP-glucose nor produced glycogen from ADP-glucose, demonstrating that the uptake of this nucleotide-sugar is CRP-cAMP regulated in E. coli. Finally, using a systematic and comprehensive gene-disrupted mutant collection of E. coli we identifi ed some genes belonging to the CRP-cAMP regulon encoding membrane proteins whose absence impair ADP-glucose transport. | Descripción: | Póster presentado en el XXXVII Congreso de la Sociedad Española de Bioquímica y Biología Molecular (SEBBM), celbrado en Granada del 9 al 12 de septiembre de 2014. | URI: | http://hdl.handle.net/10261/142193 |
Aparece en las colecciones: | (IDAB) Comunicaciones congresos |
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