Description

This is a composite part for intracellular expression of DsbC. Pynr071c is the promoter of Aldose 1-isomerase superfamily protein YNR071C. In the presence of xylose, DsbC is expressed and participates in the process of straightening.

Usage and Biology

DsbC is one of five essential protein needed for forming disulfide bonds in E.coli, functioning as disulfide bond isomerase during folding process of oxidized protein in periplasmic space. DsbC is a homodimer of size of 2x23kDa, with enzymatic activity of protein disulfide bonds isomerase and molecular chaperone. The crystal structure of DsbC shows that disulfide bonds are formed in all Cys-X-X-Cys reaction center. Through the hinge, which allows the reaction center moving relatively, a single thioredoxin-like domain is linked to dimer domain in the amino-terminal. The widely-existing uncharged seam between reaction center may participate in peptide combination and enzymatic reaction of DsbC folding enzymes. Linking DsbC with peptides rich in cysteine, we build a transporting and auxiliary binding complex with disulfide bond isomerase and short peptides DsbC is a periplasmic disulfide isomerase of Gram-negative bacteria. Its activity is only 30% of that of eukaryotic disulfide isomerase (PDI) isomerase and mercaptan oxidoreductase. However, DsbC showed more significant chaperone activity than PDI in promoting reactivation of denatured D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in vitro and inhibiting aggregation during renaturation. Like PDI, DsbC is a disulfide isomerase with chaperone activity, but it may recognize different folding intermediates. Studies have shown that PDI is linked to polypeptides containing cysteine, which can help polypeptides bind to hair and help repair hair damage. In the process of hair straightening, we need to replace the original peptides, while DsbC is small enough to enter the hair to help the new peptides bind to the hair.

Part:BBa_K3711079

Description

Usage and Biology