Abstract
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.
Item Type: | Journal article |
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Faculties: | Chemistry and Pharmacy > Department of Biochemistry |
Subjects: | 500 Science > 570 Life sciences; biology |
URN: | urn:nbn:de:bvb:19-epub-34084-1 |
ISSN: | 2211-1247 |
Language: | English |
Item ID: | 34084 |
Date Deposited: | 15. Feb 2017, 16:03 |
Last Modified: | 04. Nov 2020, 13:12 |