Chloroplast Protein Quality Control
Plants are sessile organisms that have developed very flexible strategies to cope with adverse environmental conditions as heat, cold, drought and salt stress. We study how chaperones and proteases act coordinately in the chloroplast, constituting the chloroplast protein quality control systems. In particular, Hsp70 molecular chaperone recycle damaged proteins avoiding the accumulation of toxic aggregates and cellular damage. It is known that the specificity of Hsp70 is determined by its DNAJ partners, adaptors that recognize unfolded substrates and transfer them to the chaperone for refolding. Currently we aim to unveil the specificity of the chloroplastic DNAJ proteins in order to unveil new pathways of posttranslational regulation in the chloroplast.
The chaperone system DNAJ/Hsp70 refolds protein aggregates Additionally, some DNAJ isoforms have lost the motifs required for Hsp70, acting as Hsp70-independent chaperones or assembly factors. For instance, we have recently demonstrated that SCO2 is required for the correct assembly of LHC to PSII complexes.
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