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چاپرون
Correct protein folding occurs in the endoplasmic reticulum in eukaryotes and is facilitated by a number of different proteins, including molecular chaperones, enzymes that promote disulfide bond formation, signal trans duction proteins that monitor the demand and capacity of the protein folding machinery, and proteases that clear away improperly folded or aggregated proteins (Fig. 3.29).
The overproduction of molecular chaperones and protein disulfide isomerases may increase the yield of recombinant proteins, especially those with disulfide bonds.
During synthesis on ribosomes associated with the endoplasmic reticulum (ER), nascent proteins are bound by the chaperones BiP and calnexin, which aid in the correct folding of the protein.
Higher levels of secreted products were also obtained for the recombinant proteins human erythropoietin, bovine prochymosin, and leech hirudin in S. cerevisiae cells that overexpress the chaperone BiP.
Overexpression of the molecular chaperone BiP or protein disulfide iso merase increased the secretion of some heterologous protein; however, overexpression of a single chaperone may not have the desired outcome and, in some instances, may increase the degradation of the target protein.
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