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Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation

Komar, Anton A, Lesnik, Thierry, Reiss, Claude·1999·FEBS Letters

Abstract

To investigate the possible influence of the local rates of translation on protein folding, 16 consecutive rare (in Escherichia coli) codons in the chloramphenicol acetyltransferase (CAT) gene have been replaced by frequent ones. Site‐directed silent mutagenesis reduced the pauses in translation of CAT in E. coli S30 extract cell‐free system and led to the acceleration of the overall rate of CAT protein synthesis. At the same time, the silently mutated protein (with unaltered protein sequence) synthesized in the E. coli S30 extract system was shown to possess 20% lower specific activity. The data suggest that kinetics of protein translation can affect the in vivo protein‐folding pathway, leading to increased levels of protein misfolding.

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Metadata

Authors
Komar, A. A., Lesnik, T., & Reiss, C.
Venue
FEBS Letters
Publisher
Wiley
Published
1999-11-30
Volume
462
Issue
3
Pages
387-391
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2149424410
Cited by
385
References
0
FWCI
1.41
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. https://app.cochat.ai/papers/10.1016/s0014-5793(99)01566-5
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Komar, A. A., Lesnik, T., & Reiss, C. (1999). Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. FEBS Letters. https://doi.org/10.1016/s0014-5793(99)01566-5

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