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Quantifying elongation rhythm during full-length protein synthesis
- Source :
- Journal of the American Chemical Society. 135(30)
- Publication Year :
- 2013
-
Abstract
- Pauses regulate the rhythm of ribosomal protein synthesis. Mutations disrupting even minor pauses can give rise to improperly formed proteins and human disease. Such minor pauses are difficult to characterize by ensemble methods, but can be readily examined by single-molecule (sm) approaches. Here we use smFRET to carry out real-time monitoring of the expression of a full-length protein, the green fluorescent protein variant Emerald GFP. We demonstrate significant correlations between measured elongation rates and codon and isoacceptor tRNA usage, and provide a quantitative estimate of the effect on elongation rate of replacing a codon recognizing an abundant tRNA with a synonymous codon cognate to a rarer tRNA. Our results suggest that tRNA selection plays an important general role in modulating the rates and rhythms of protein synthesis, potentially influencing simultaneous co-translational processes such as folding and chemical modification.
- Subjects :
- Silent mutation
Models, Molecular
Protein Conformation
Green Fluorescent Proteins
Molecular Sequence Data
Peptide Chain Elongation, Translational
Biochemistry
Ribosome
Catalysis
Article
Colloid and Surface Chemistry
Protein structure
RNA, Transfer
Ribosomal protein
Protein biosynthesis
Fluorescence Resonance Energy Transfer
Amino Acid Sequence
Codon
Chemistry
General Chemistry
Molecular biology
Peptide Fragments
Cell biology
Codon usage bias
Transfer RNA
Mutation
Synonymous substitution
Ribosomes
Subjects
Details
- ISSN :
- 15205126
- Volume :
- 135
- Issue :
- 30
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi.dedup.....2b01663bd3ac6e4d7d1567f63e2ef6fc