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This project seeks to systematically define the functions and regulatory networks mediated by the protein disulfide isomerase (PDI) gene family. PDIs are highly abundant proteins and are known to oxidoreductase known to assist in the co- and post-translational processing and folding of newly synthesized secretory proteins in the lumen of the endoplasmic reticulum (ER). They catalyze the reversible formation and isomerization of disulfide bonds necessary for the proper folding, assembly, activity, and secretion of numerous enzymes and structural proteins. There are 11 members of the PDI gene family in Arabidopsis (see Table-1). This research aims to elucidate the function of all members of the PDI family by determining the subcellular locations and tissue-specific expression levels of each PDI and by identifying a wide range of substrates and partners with which each PDI interacts. We will also analyze the available T-DNA knockout mutants and construct double and triple mutants and pdi over-expresser lines. PDI's have also evolved novel cellular functions, as single enzymes and as subunits of protein complexes, in chloroplasts, mitochondria, nuclei, and vacuoles. Through redox-based mechanisms involving their thioredoxin domains, they are implicated in regulating transcription, translation, organelle biogenesis, photosynthetic efficiency, and cell differentiation in a variety of tissues and stages of development. The primary structure of the PDI family in Arabidopsis with their thiroredoxin motifs and transit peptide domains are shown below.
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