Journal
CELL REPORTS
Volume 12, Issue 10, Pages 1533-1540Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2015.07.065
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Funding
- Swedish Foundation for Strategic Research
- European Research Council [ERC-2008-AdG 232648]
- Swedish Cancer Foundation
- Swedish Research Council
- Knut and Alice Wallenberg Foundation
- NIH [GM51266, GM09968701]
- Wenner-Gren Foundations
- Early Postdoc Mobility Fellowship from Swiss National Science Foundation
- Novartis Foundation
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At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of co-translational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.
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