Next Article in Journal
Seed Priming with Jasmonic Acid Counteracts Root Knot Nematode Infection in Tomato by Modulating the Activity and Expression of Antioxidative Enzymes
Next Article in Special Issue
Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution
Previous Article in Journal
The Role of Urocortins in Intracerebral Hemorrhage
Previous Article in Special Issue
Structural and Biophysical Analyses of Human N-Myc Downstream-Regulated Gene 3 (NDRG3) Protein

Cotranslational Folding of Proteins on the Ribosome

Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany
Authors to whom correspondence should be addressed.
Biomolecules 2020, 10(1), 97;
Received: 5 December 2019 / Revised: 20 December 2019 / Accepted: 25 December 2019 / Published: 7 January 2020
Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different ways. In this review, we summarize the recent examples of how translation affects folding of single-domain, multiple-domain and oligomeric proteins. The vectorial nature of translation, the spatial constraints of the exit tunnel, and the electrostatic properties of the ribosome-nascent peptide complex define the onset of early folding events. The ribosome can facilitate protein compaction, induce the formation of intermediates that are not observed in solution, or delay the onset of folding. Examples of single-domain proteins suggest that early compaction events can define the folding pathway for some types of domain structures. Folding of multi-domain proteins proceeds in a domain-wise fashion, with each domain having its role in stabilizing or destabilizing neighboring domains. Finally, the assembly of protein complexes can also begin cotranslationally. In all these cases, the ribosome helps the nascent protein to attain a native fold and avoid the kinetic traps of misfolding. View Full-Text
Keywords: cotranslational protein folding; ribosome; polypeptide exit tunnel; nascent polypeptides; translation; protein synthesis cotranslational protein folding; ribosome; polypeptide exit tunnel; nascent polypeptides; translation; protein synthesis
Show Figures

Figure 1

MDPI and ACS Style

Liutkute, M.; Samatova, E.; Rodnina, M.V. Cotranslational Folding of Proteins on the Ribosome. Biomolecules 2020, 10, 97.

AMA Style

Liutkute M, Samatova E, Rodnina MV. Cotranslational Folding of Proteins on the Ribosome. Biomolecules. 2020; 10(1):97.

Chicago/Turabian Style

Liutkute, Marija, Ekaterina Samatova, and Marina V. Rodnina 2020. "Cotranslational Folding of Proteins on the Ribosome" Biomolecules 10, no. 1: 97.

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop