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Mimicking cotranslational folding of prosubtilisin E in vitro.
- Source :
-
Journal of Biochemistry . May2020, Vol. 167 Issue 5, p473-482. 10p. - Publication Year :
- 2020
-
Abstract
- 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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *TERTIARY structure
*RIBOSOMES
*POLYPEPTIDES
*GENETIC translation
Subjects
Details
- Language :
- English
- ISSN :
- 0021924X
- Volume :
- 167
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 142976148
- Full Text :
- https://doi.org/10.1093/jb/mvaa004