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  Synonymous codons direct cotranslational folding toward different protein conformations.

Buhr, F., Jha, S., Thommen, M., Mittelstät, J., Kutz, F., Schwalbe, H., et al. (2016). Synonymous codons direct cotranslational folding toward different protein conformations. Molecular Cell, 61(3), 341-351. doi:10.1016/j.molcel.2016.01.008.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-03EF-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-5FF0-D
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 Creators:
Buhr, F., Author
Jha, S., Author
Thommen, M.1, Author              
Mittelstät, J.1, Author              
Kutz, F., Author
Schwalbe, H., Author
Rodnina, M. V.1, Author              
Komar, A. A., Author
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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 Abstract: In all genomes, most amino acids are encoded by more than one codon. Synonymous codons can modulate protein production and folding, but the mechanism connecting codon usage to protein homeostasis is not known. Here we show that synonymous codon variants in the gene encoding gamma-B crystallin, a mammalian eye-lens protein, modulate the rates of translation and cotranslational folding of protein domains monitored in real time by Forster resonance energy transfer and fluorescence-intensity changes. Gamma-B crystallins produced from mRNAs with changed codon bias have the same amino acid sequence but attain different conformations, as indicated by altered invivo stability and invitro protease resistance. 2D NMR spectroscopic data suggest that structural differences are associated with different cysteine oxidation states of the purified proteins, providing a link between translation, folding, and the structures of isolated proteins. Thus, synonymous codons provide a secondary code for protein folding in the cell.

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Language(s): eng - English
 Dates: 2016-02-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2016.01.008
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 61 (3) Sequence Number: - Start / End Page: 341 - 351 Identifier: -