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Cotranslational folding of proteins
V A Kolb1, E V Makeyev, A Kommer
1Institute of Protein Research, Academy of Sciences of Russia, Moscow Region, Russia.
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|November 1, 1995
Summary
Protein folding can occur on the ribosome, challenging the idea that it only happens after translation. This cotranslational folding process allows nascent proteins to attain their native structure and biological activity during synthesis.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- While many unfolded proteins can refold upon denaturant removal, this in vitro process doesn't fully represent intracellular protein folding.
- The discovery of molecular chaperones influenced the view that protein folding in vivo is primarily a post-translational event.
- Recent research suggests molecular chaperones play a role in modulating protein folding, potentially supporting post-translational folding.
Purpose of the Study:
- To investigate whether nascent proteins can achieve their final native structure and biological activity while still being synthesized on the ribosome.
- To challenge the prevailing hypothesis that protein folding is exclusively a post-translational process.
- To provide evidence supporting the cotranslational folding hypothesis.
Main Methods:
- The study discusses existing data and recent publications related to protein folding mechanisms.
- Analysis of experimental evidence supporting the attainment of native structure and biological activity on the ribosome.
- Review of findings on molecular chaperone action and their implications for in vivo folding.
Main Results:
- Data indicates that nascent proteins can achieve their final native structure on the ribosome.
- Biological activity can be attained by proteins during their synthesis on the ribosome.
- The findings suggest that protein folding can occur concurrently with translation.
Conclusions:
- The study supports the cotranslational folding hypothesis, where protein folding occurs during translation.
- Protein folding in vivo is not solely a post-translational process.
- Nascent proteins can acquire their functional conformation while still attached to the ribosome.