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The Ribosome Cooperates with a Chaperone to Guide Multi-domain Protein Folding
- Source :
- Molecular Cell. 74:310-319.e7
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- Multi-domain proteins, containing several structural units within a single polypeptide, constitute a large fraction of all proteomes. Co-translational folding is assumed to simplify the conformational search problem for large proteins, but the events leading to correctly folded, functional structures remain poorly characterized. Similarly, how the ribosome and molecular chaperones promote efficient folding remains obscure. Using optical tweezers, we have dissected early folding events of nascent elongation factor G, a multi-domain protein that requires chaperones for folding. The ribosome and the chaperone trigger factor reduce inter-domain misfolding, permitting folding of the N-terminal G-domain. Successful completion of this step is a crucial prerequisite for folding of the next domain. Unexpectedly, co-translational folding does not proceed unidirectionally: emerging unfolded polypeptide can denature an already folded domain. Trigger factor, but not the ribosome, protects against denaturation. The chaperone thus serves a previously unappreciated function, helping multi-domain proteins overcome inherent challenges during co-translational folding.
- Subjects :
- Protein Folding
Optical Tweezers
Proteome
Protein Conformation
Ribosome
Article
03 medical and health sciences
0302 clinical medicine
Protein Domains
Protein biosynthesis
Denaturation (biochemistry)
Molecular Biology
030304 developmental biology
0303 health sciences
biology
Elongation Factor G
Cell Biology
Peptide Elongation Factor G
Cell biology
Multi domain
Protein Biosynthesis
Chaperone (protein)
biology.protein
Protein folding
Peptides
Ribosomes
030217 neurology & neurosurgery
Molecular Chaperones
Subjects
Details
- ISSN :
- 10972765
- Volume :
- 74
- Database :
- OpenAIRE
- Journal :
- Molecular Cell
- Accession number :
- edsair.doi.dedup.....063d2f63e7c1e9316fa547f624825ae7