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Mermans D, Nicolaus F, Baygin A, von Heijne G
FEBS Lett. 597 (10) 1355-1362 [2023-05-00; online 2022-12-22]
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.
PubMed 36520514
DOI 10.1002/1873-3468.14562
Crossref 10.1002/1873-3468.14562