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Functional dependence between septal protein SepJ from Anabaena sp. Strain PCC 7120 and an amino acid ABC-type uptake transporter

Opened Access Functional dependence between septal protein SepJ from Anabaena sp. Strain PCC 7120 and an amino acid ABC-type uptake transporter

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Autor: Escudero, Leticia
Mariscal, Vicente
Flores García, Enrique
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2015
Publicado en: Journal of Bacteriology, 197 (16), 2721-2730.
Tipo de documento: Artículo
Resumen: In the diazotrophic filaments of heterocyst-forming cyanobacteria, two different cell types, the CO2-fixing vegetative cells and the N2-fixing heterocysts, exchange nutrients, including some amino acids. In the model organism Anabaena sp. strain PCC 7120, the SepJ protein, composed of periplasmic and integral membrane (permease) sections, is located at the intercellular septa joining adjacent cells in the filament. The unicellular cyanobacterium Synechococcus elongatus strain PCC 7942 bears a gene, Synpcc7942_1024 (here designated dmeA), encoding a permease homologous to the SepJ permease domain. Synechococcus strains lacking dmeA or lacking dmeA and expressing Anabaena sepJ were constructed. The Synechococcus dmeA mutant showed a significant 22 to 32% decrease in the uptake of aspartate, glutamate, and glutamine, a phenotype that could be partially complemented by Anabaena sepJ. Synechococcus mutants of an ATP-binding-cassette (ABC)-type transporter for polar amino acids showed>98% d...
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Cita: Escudero, L., Mariscal, V. y Flores García, E. (2015). Functional dependence between septal protein SepJ from Anabaena sp. Strain PCC 7120 and an amino acid ABC-type uptake transporter. Journal of Bacteriology, 197 (16), 2721-2730.
Tamaño: 592.5Kb
Formato: PDF

URI: http://hdl.handle.net/11441/62809

DOI: 10.1128/JB.00289-15

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