Recombinant protein folding and misfolding in Escherichia coli.
The past 20 years have seen enormous progress in the understanding of the mechanisms used by the enteric bacterium Escherichia coli to promote protein folding, support protein translocation and handle protein misfolding. Insights from these studies have been exploited to tackle the problems of inclusion body formation, proteolytic degradation and disulfide bond generation that have long impeded the production of complex heterologous proteins in a properly folded and biologically active form. The application of this information to industrial processes, together with emerging strategies for creating designer folding modulators and performing glycosylation all but guarantee that E. coli will remain an important host for the production of both commodity and high value added proteins.
Baneyx
François
F
Departments of Chemical Engineering and Bioengineering, University of Washington, Box 351750, Seattle, Washington 98195, USA. baneyx@u.washington.edu
Mujacic
Mirna
M
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D002479:Inclusion Bodies / Q000235:genetics / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods; D017510:Protein Folding; D021381:Protein Transport / Q000502:physiology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins