Target molecule recognition and redox regulation by the chloroplast thioredoxin

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A. Interaction between thioredoxins and their targetsWe first studied the interaction between the plant cytosolic thioredoxin (Trx-hl) and the cytosolic malate dehydrogenase and successfully revealed that this malate dehydrogenase is the newly identified Trx-target protein. We then studied the counterpart proteins of thioredoxins from photosynthetic bacteria and cyanobacteria to reveal the multiplicity of the role of thioredoxins. In addition, we clarified the difference of the roles of two redox-equivalent supply pathways, ferredoxin-dependent thioredoxin reductase pathway and NADPH dependent thioredoxin reductase pathway in the cyanobacteria Synechocystis sp. PCC6803.B. Structural analysis of the protein-protein interaction between thioredoxins and their targets.One of the most interesting questions are why thioredoxins can recognize various proteins, which contains the redox sensitive disulfide bond on the molecular surface, as their target. In order to answer this query, we tried to solve the crystal structures of the thioredoxin-target protein cocomplex using X-ray crystallography. Although we have tried to efficiently obtain the co-complexexes under the various chemical conditions, we failed to set up the suitable experimental conditions to obtain the complex proteins during the research term and could not solve any structures which should be important to know the amino acid residues which may involve into the interaction.