Repositorio de producción científica de la Universidad de Sevilla

Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different

Opened Access Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different

Citas

buscar en

Estadísticas
Icon
Exportar a
Autor: Florencio Bellido, Francisco Javier
Lindahl, Anna Marika
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2003
Tipo de documento: Artículo
Resumen: Light-dependent regulation of a growing number of chloroplast enzymatic activities has been found to occur through the reversible reduction of intra- or intermolecular disulphides by thioredoxins. In cyanobacteria, despite their similarity to chloroplasts, no proteins have hitherto been shown to interact with thioredoxins, and the role of the cyanobacterial ferredoxin/thioredoxin system has remained obscure. By using an immobilized cysteine 35-to-serine site-directed mutant of the Synechocystis sp. PCC 6803 thioredoxin TrxA as bait, we screened the Synechocystis cytosolic and peripheral membrane protein complements for proteins interacting with TrxA. The covalent bond between the isolated target proteins and mutated TrxA was confirmed by nonreducing/reducing two-dimensional SDS/PAGE. Thus, we have identified 18 cytosolic proteins and 8 membrane-associated proteins as candidate thioredoxin substrates. Twenty of these proteins have not previously been associated with thioredoxin-mediate...
[Ver más]
Tamaño: 352.0Kb
Formato: PDF

URI: https://hdl.handle.net/11441/69622

DOI: 10.1073/pnas.2534397100

Ver versión del editor

Mostrar el registro completo del ítem


Esta obra está bajo una Licencia Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 Internacional

Este registro aparece en las siguientes colecciones