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- W2789535447 abstract "All cells rely on protein folding to support and sustain life, yet protein folding pathways in vivo are not well understood. Inside E. Coli cells, proteins are produced by ribosomes in the presence of the trigger factor and DnaK molecular chaperones. Prior studies established that both the ribosome and molecular chaperones facilitate in vivo protein folding. However, it has not yet been possible to determine their independent roles since cells cannot survive at temperatures over 30°C when the genes for trigger factor and DnaK have been concurrently knocked out. In this investigation, we attain the latter important yet elusive experimental condition by biosynthesizing a model protein in an E. Coli cell-free system derived from a trigger factor- deleted cell strain in the presence of an in-house-designed peptide inhibitor of DnaK. We show that the process of being translated through the ribosome is sufficient to grant solubility to the de novo-synthesized protein at submicromolar protein concentrations. The cotranslationally acquired structure favors proper folding but it is not a sufficient condition to ensure it. We employed time-resolved fluorescence anisotropy in the frequency-domain in combination with multidimensional NMR spectroscopy to study the quality of the de novo-produced protein. We found that even soluble ribosome-released proteins may be improperly folded, and minimal concentrations of molecular chaperones are required to ensure proper folding." @default.
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- W2789535447 date "2018-02-01" @default.
- W2789535447 modified "2023-10-18" @default.
- W2789535447 title "Teasing Apart the Role of the Ribosome and Molecular Chaperones in Cellular Protein Folding" @default.
- W2789535447 doi "https://doi.org/10.1016/j.bpj.2017.11.2293" @default.
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