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  Gradual compaction of nascent peptide during cotranslational folding on the ribosome

Liutkute, M., Maiti, M., Samatova, E. N., Enderlein, J., & Rodnina, M. V. (2020). Gradual compaction of nascent peptide during cotranslational folding on the ribosome. eLife, 9: e60895. doi:10.7554/eLife.60895.

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Liutkute, M.1, Author                 
Maiti, M.1, Author                 
Samatova, E. N.1, Author                 
Enderlein, J., Author
Rodnina, M. V.2, Author           
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1Department of Physical Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578598              
2Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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 Abstract: Nascent polypeptides begin to fold in the constrained space of the ribosomal peptide exit tunnel. Here we use force-profile analysis (FPA) and photo-induced energy-transfer fluorescence correlation spectroscopy (PET-FCS) to show how a small α-helical domain, the N-terminal domain of HemK, folds cotranslationally. Compaction starts vectorially as soon as the first α-helical segments are synthesized. As nascent chain grows, emerging helical segments dock onto each other and continue to rearrange at the vicinity of the ribosome. Inside or in the proximity of the ribosome, the nascent peptide undergoes structural fluctuations on the µs time scale. The fluctuations slow down as the domain moves away from the ribosome. Mutations that destabilize the packing of the domain’s hydrophobic core have little effect on folding within the exit tunnel, but abolish the final domain stabilization. The results show the power of FPA and PET-FCS in solving the trajectory of cotranslational protein folding and in characterizing the dynamic properties of folding intermediates.

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Language(s): eng - English
 Dates: 2020-10-27
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.7554/eLife.60895
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Title: eLife
Source Genre: Journal
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Pages: 21 Volume / Issue: 9 Sequence Number: e60895 Start / End Page: - Identifier: -