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Slowing bacterial translation speed enhances eukaryotic protein folding efficiency
- Source :
- Journal of molecular biology. 396(5)
- Publication Year :
- 2009
-
Abstract
- The mechanisms for de novo protein folding differ significantly between bacteria and eukaryotes, as evidenced by the often observed poor yields of native eukaryotic proteins upon recombinant production in bacterial systems. Polypeptide synthesis rates are faster in bacteria than in eukaryotes, but the effects of general variations in translation rates on protein folding efficiency have remained largely unexplored. By employing Escherichia coli cells with mutant ribosomes whose translation speed can be modulated, we show here that reducing polypeptide elongation rates leads to enhanced folding of diverse proteins of eukaryotic origin. These results suggest that in eukaryotes, protein folding necessitates slow translation rates. In contrast, folding in bacteria appears to be uncoupled from protein synthesis, explaining our findings that a generalized reduction in translation speed does not adversely impact the folding of the endogenous bacterial proteome. Utilization of this strategy has allowed the production of a native eukaryotic multidomain protein that has been previously unattainable in bacterial systems and may constitute a general alternative to the production of aggregation-prone recombinant proteins.
- Subjects :
- Ribosomal Proteins
Protein Folding
Green Fluorescent Proteins
Peptide Chain Elongation, Translational
Biology
In Vitro Techniques
Eukaryotic translation
Structural Biology
Bacterial transcription
Luciferases, Firefly
Prokaryotic translation
Protein biosynthesis
Escherichia coli
Animals
Molecular Biology
DNA Primers
'de novo' protein folding
Base Sequence
Escherichia coli Proteins
Apraxia, Ideomotor
Recombinant Proteins
EIF4EBP1
Biochemistry
Genes, Bacterial
Chaperone (protein)
Protein Biosynthesis
Mutation
biology.protein
Protein folding
Protein Multimerization
Subjects
Details
- ISSN :
- 10898638
- Volume :
- 396
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Journal of molecular biology
- Accession number :
- edsair.doi.dedup.....0d95b2ed686dcecc14a45adfaa87fae3