TY  - JOUR
AU  - Wruck, Florian
AU  - Tian, Pengfei
AU  - Kudva, Renuka
AU  - Best, Robert B.
AU  - von Heijne, Gunnar
AU  - Tans, Sander J.
AU  - Katranidis, Alexandros
TI  - The ribosome modulates folding inside the ribosomal exit tunnel
JO  - Communications biology
VL  - 4
IS  - 1
SN  - 2399-3642
CY  - London
PB  - Springer Nature
M1  - FZJ-2021-02076
SP  - 523
PY  - 2021
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:33953328
UR  - <Go to ISI:>//WOS:000656248000007
DO  - DOI:10.1038/s42003-021-02055-8
UR  - https://juser.fz-juelich.de/record/892430
ER  -