recombinantproteinfoldingandmisfloding英文学习资料.pdfVIP

R E V I E W y Recombinant protein folding and misfolding g o l o n h c in Escherichia coli e t o i b e r François Baneyx Mirna Mujacic u t a n / m o The past 20 years have seen enormous progress in the understanding of the mechanisms used by the enteric bacterium c . e Escherichia coli to promote protein folding, support protein translocation and handle protein misfolding. Insights from these r u t studies have been exploited to tackle the problems of inclusion body formation, proteolytic degradation and disulfide bond a n w. generation that have long impeded the production of complex heterologous proteins in a properly folded and biologically active w form. The application of this information to industrial processes, together with emerging strategies for creating designer folding w / / modulators and performing glycosylation all but guarantee that E. coli will remain an important host for the production of both : p t commodity and high value added proteins. t h p u o 2 r The enteric bacterium Escherichia coli is one of the most extensively the ribosome every 35 seconds , an environment where macromole- G g used prokaryotic organisms for genetic manipulations and for the cule concentration can reach 300–400 mg/ml (ref. 3), protein folding is n i industrial production of proteins of therapeutic or commercial inter- an extraordinary challenge. In general, small (100 residues), single h s est. Compared with other established and emerging expression domain host proteins efficiently reach a native conformation owing to i l b systems1