Journal Article

FZJ-2021-02076

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The ribosome modulates folding inside the ribosomal exit tunnel

Wruck, F. ; Tian, P. ; Kudva, R. ; Best, R. B. ; von Heijne, G. ; Tans, S. J. ; Katranidis, A. (Corresponding author)FZJ*

2021
Springer Nature London

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Please use a persistent id in citations: http://hdl.handle.net/2128/28656  doi:10.1038/s42003-021-02055-8

Abstract: Proteins commonly fold co-translationally at the ribosome, while the nascent chain emerges from the ribosomal exit tunnel. Protein domains that are sufficiently small can even fold while still located inside the tunnel. However, the effect of the tunnel on the folding dynamics of these domains is not well understood. Here, we combine optical tweezers with single-molecule FRET and molecular dynamics simulations to investigate folding of the small zinc-finger domain ADR1a inside and at the vestibule of the ribosomal tunnel. The tunnel is found to accelerate folding and stabilize the folded state, reminiscent of the effects of chaperonins. However, a simple mechanism involving stabilization by confinement does not explain the results. Instead, it appears that electrostatic interactions between the protein and ribosome contribute to the observed folding acceleration and stabilization of ADR1a.

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Contributing Institute(s):

1. Zelluläre Strukturbiologie (IBI-6)

Research Program(s):

1. 5352 - Understanding the Functionality of Soft Matter and Biomolecular Systems (POF4-535) (POF4-535)
2. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2021

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