Mimicking cotranslational folding of prosubtilisin E in vitro

Sung Gun Kim, Yu Jen Chen, Liliana Falzon, Jean Baum, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Nascent polypeptides are synthesized on ribosomes starting at the N-terminus and simultaneously begin to fold during translation. We constructed N-terminal fragments of prosubtilisin E containing an intramolecular chaperone (IMC) at N-terminus to mimic cotranslational folding intermediates of prosubtilisin. The IMC-fragments of prosubtilisin exhibited progressive enhancement of their secondary structures and thermostabilities with increasing polypeptide length. However, even the largest IMC-fragment with 72 residues truncated from the C-terminus behaved as a molten globule, indicating the requirement of the C-terminal region to have a stable tertiary structure. Furthermore, truncation of the IMC in the IMC-fragments resulted in aggregation, suggesting that the IMC plays a crucial role to prevent misfolding and aggregation of cotranslational folding intermediates during translation of prosubtilisin polypeptide.

Original languageEnglish (US)
Pages (from-to)473-482
Number of pages10
JournalJournal of Biochemistry
Issue number5
StatePublished - May 1 2020

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


  • Cotranslational folding intermediate
  • Intramolecular chaperone
  • Prosubtilisin E
  • Secondary structure


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