Mimicking cotranslational folding of prosubtilisin E in vitro
| Autor: | Masayori Inouye, Yu-Jen Chen, Sung-Gun Kim, Liliana Falzon, Jean Baum |
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| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Enzyme Precursors Protein Folding biology Protein Stability Chemistry Subtilisin General Medicine In Vitro Techniques Biochemistry Ribosome Peptide Fragments Protein Structure Secondary Molten globule In vitro Protein tertiary structure Chaperone (protein) biology.protein Biophysics Prosubtilisin E Subtilisins Molecular Biology Protein secondary structure Bacillus subtilis Molecular Chaperones |
| Zdroj: | The Journal of Biochemistry. 167:473-482 |
| ISSN: | 1756-2651 0021-924X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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