Cotranslational folding of human growth hormone in vitro and in Escherichia coli.
cotranslational protein folding
human growth hormone
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
05 2023
05 2023
Historique:
revised:
01
12
2022
received:
01
09
2022
accepted:
09
12
2022
medline:
26
5
2023
pubmed:
16
12
2022
entrez:
15
12
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 36520514
doi: 10.1002/1873-3468.14562
doi:
Substances chimiques
Human Growth Hormone
12629-01-5
Molecular Chaperones
0
Escherichia coli Proteins
0
Types de publication
Letter
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1355-1362Informations de copyright
© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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