Cotranslational Protein Folding inside the Ribosome Exit Tunnel
Number of Authors: 12
2015 (English)In: Cell reports, ISSN 2211-1247, E-ISSN 2211-1247, Vol. 12, no 10, 1533-1540 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2015. Vol. 12, no 10, 1533-1540 p.
Ribosome, Protein Folding, Cotranslational Folding, Translation, SecM, Cryo-EM
Biochemistry and Molecular Biology Cell Biology Biophysics
Research subject Biochemistry
IdentifiersURN: urn:nbn:se:su:diva-121762DOI: 10.1016/j.celrep.2015.07.065ISI: 000360965500002OAI: oai:DiVA.org:su-121762DiVA: diva2:861205