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      A cytosolic thioredoxin acts as a molecular chaperone for peroxisome matrix proteins as well as antioxidant in peroxisome.

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          Abstract

          Thioredoxin (TRX) is a disulfide reductase present ubiquitously in all taxa and plays an important role as a regulator of cellular redox state. Recently, a redox-independent, chaperone function has also been reported for some thioredoxins. We previously identified nodulin-35, the subunit of soybean uricase, as an interacting target of a cytosolic soybean thioredoxin, GmTRX. Here we report the further characterization of the interaction, which turns out to be independent of the disulfide reductase function and results in the co-localization of GmTRX and nodulin-35 in peroxisomes, suggesting a possible function of GmTRX in peroxisomes. In addition, the chaperone function of GmTRX was demonstrated in in vitro molecular chaperone activity assays including the thermal denaturation assay and malate dehydrogenase aggregation assay. Our results demonstrate that the target of GmTRX is not only confined to the nodulin-35, but many other peroxisomal proteins, including catalase (AtCAT), transthyretin-like protein 1 (AtTTL1), and acyl-coenzyme A oxidase 4 (AtACX4), also interact with the GmTRX. Together with an increased uricase activity of nodulin-35 and reduced ROS accumulation observed in the presence of GmTRX in our results, especially under heat shock and oxidative stress conditions, it appears that GmTRX represents a novel thioredoxin that is co-localized to the peroxisomes, possibly providing functional integrity to peroxisomal proteins.

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          Author and article information

          Journal
          Mol. Cells
          Molecules and cells
          Korean Society for Molecular and Cellular Biology
          0219-1032
          1016-8478
          2015
          : 38
          : 2
          Affiliations
          [1 ] Department of Biological Science, Sookmyung Women's University, Seoul 140-742, Korea.
          [2 ] Department of Plant Science, Seoul National University, Seoul 151-742, Korea.
          Article
          molcell-38-2-187
          10.14348/molcells.2015.2255
          4332030
          26013260
          68446bd7-a554-45ad-98cd-3e28f675bcd7

          peroxisome, chaperone, thioredoxin, uricase

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