Folding at the birth of the nascent chain: coordinating translation with co-translational folding
- In the living cells, the folding of many proteins is largely believed to begin co-translationally, during their biosynthesis at the ribosomes. In the ribosomal tunnel, the nascent peptide may establish local interactions and stabilize alpha-helical structures. Long-range contacts are more likely outside the ribosomes after release of larger segments of the nascent chain. Examples suggest that domains can attain native-like structure on the ribosome with and without population of folding intermediates. The co-translational folding is limited by the speed of the gradual extrusion of the nascent peptide which imposes conformational restraints on its folding landscape. Recent experimental and in silico modeling studies indicate that translation kinetics fine-tunes co-translational folding by providing a time delay for sequential folding of distinct portions of the nascent chain.
Author details: | Gong Zhang, Zoya Ignatova |
---|---|
DOI: | https://doi.org/10.1016/j.sbi.2010.10.008 |
ISSN: | 0959-440X |
Title of parent work (English): | Current opinion in structural biology : review of all advances ; evaluation of key references ; comprehensive listing of papers |
Publisher: | Elsevier |
Place of publishing: | London |
Publication type: | Review |
Language: | English |
Year of first publication: | 2011 |
Publication year: | 2011 |
Release date: | 2017/03/26 |
Volume: | 21 |
Issue: | 1 |
Number of pages: | 7 |
First page: | 25 |
Last Page: | 31 |
Funding institution: | SysMO; Deutsche Forschungsgemeinschaft [IG 73/10-1] |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
Peer review: | Referiert |