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Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations.

Florian Buhr¹, Sujata Jha², Michael Thommen³

¹Center for Biomolecular Magnetic Resonance, Institute of Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-Universität Frankfurt am Main, 60438 Frankfurt am Main, Germany.

|February 6, 2016

Summary

This summary is machine-generated.

Synonymous codons, which code for the same amino acid, influence protein folding and stability. This study reveals a secondary genetic code where codon bias affects protein structure and homeostasis.

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Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

Most amino acids are encoded by multiple synonymous codons.
The precise mechanism linking codon usage to protein homeostasis remains unclear.
Synonymous codons are known to influence protein production and folding dynamics.

Purpose of the Study:

To investigate how synonymous codon variants affect protein folding and stability.
To elucidate the connection between codon usage, translation rates, and cotranslational folding.
To determine if codon bias can alter protein conformation and cellular homeostasis.

Main Methods:

Real-time monitoring of protein domain folding using Förster resonance energy transfer (FRET) and fluorescence intensity.
Analysis of protein stability in vivo and protease resistance in vitro.
Two-dimensional Nuclear Magnetic Resonance (2D NMR) spectroscopy to assess protein structure.

Main Results:

Synonymous codon variants in the gamma-B crystallin gene modulated translation and cotranslational folding rates.
Altered codon bias resulted in gamma-B crystallins with different conformations, stability, and protease resistance.
2D NMR data indicated structural differences linked to cysteine oxidation states, connecting translation, folding, and protein structure.

Conclusions:

Synonymous codons constitute a secondary code that influences protein folding.
Codon usage impacts protein structure, stability, and potentially cellular homeostasis.
This finding provides a novel link between genetic code, protein biosynthesis, and protein structure.