Structural highlights
Function
[ADR1_YEAST] Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).
Publication Abstract from PubMed
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 cotranslational 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.
Cotranslational Protein Folding inside the Ribosome Exit Tunnel.,Nilsson OB, Hedman R, Marino J, Wickles S, Bischoff L, Johansson M, Muller-Lucks A, Trovato F, Puglisi JD, O'Brien EP, Beckmann R, von Heijne G Cell Rep. 2015 Sep 8;12(10):1533-40. doi: 10.1016/j.celrep.2015.07.065. Epub 2015, Aug 28. PMID:26321634[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nilsson OB, Hedman R, Marino J, Wickles S, Bischoff L, Johansson M, Muller-Lucks A, Trovato F, Puglisi JD, O'Brien EP, Beckmann R, von Heijne G. Cotranslational Protein Folding inside the Ribosome Exit Tunnel. Cell Rep. 2015 Sep 8;12(10):1533-40. doi: 10.1016/j.celrep.2015.07.065. Epub 2015, Aug 28. PMID:26321634 doi:http://dx.doi.org/10.1016/j.celrep.2015.07.065
