Cotranslational folding of human growth hormone in vitro and in Escherichia coli

Human growth hormone (hGH) is a four-helix bundle protein of considerable pharmacological interest. Recombinant hGH is produced in bacteria, yet little is known about its folding during expression in Escherichia coli. We have studied the cotranslational folding of hGH using force profile analysis (FPA), both during in vitro translation in the absence and presence of the chaperone trigger factor (TF), and when expressed in E. coli. We find that the main folding transition starts before hGH is completely released from the ribosome, and that it can interact with TF and possibly other chaperones.

Automated summary

Human growth hormone (hGH) is a protein with four helix bundles and has pharmacological interest. This study investigates the folding of hGH during expression in Escherichia coli, both in vitro translation with or without the chaperone trigger factor (TF) and in E. coli. The findings suggest that hGH begins folding before it is fully released from the ribosome and may interact with TF and other chaperones.