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@ARTICLE{Till:1044990,
author = {Till, Katharina and Seinen, Anne-Bart and Wruck, Florian
and Sunderlikova, Vanda and Galmozzi, Carla V. and
Katranidis, Alexandros and Bukau, Bernd and Kramer, Günter
and Tans, Sander J.},
title = {{T}rigger factor accelerates nascent chain compaction and
folding},
journal = {Proceedings of the National Academy of Sciences of the
United States of America},
volume = {122},
number = {30},
issn = {0027-8424},
address = {Washington, DC},
publisher = {National Acad. of Sciences},
reportid = {FZJ-2025-03475},
pages = {e2422678122},
year = {2025},
abstract = {Recent work indicates that many chaperones bind protein
chains already during their translation by ribosomes. While
chaperones are thought to merely “hold” the nascent
protein chains, current methods cannot study their
conformational changes. We simultaneously image single
chaperone binding and detect nascent protein conformation.
We show that the chaperone trigger factor accelerates the
folding of proteins as they emerge from the ribosome and
reveal the mechanism: By enhancing the polypeptide collapse,
it pushes residues together. Our mechanism promotes folding
to occur cotranslationally, impacts the many processes that
depend on it, like cotranslational protein assembly,
translation arrest mitigation, and aggregation suppression,
and can help explain how trigger factor interacts with
downstream chaperones and how cells produce proteins with
limited errors.},
cin = {ER-C-3},
ddc = {500},
cid = {I:(DE-Juel1)ER-C-3-20170113},
pnm = {5352 - Understanding the Functionality of Soft Matter and
Biomolecular Systems (POF4-535) / 5241 - Molecular
Information Processing in Cellular Systems (POF4-524)},
pid = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
typ = {PUB:(DE-HGF)16},
pubmed = {40711920},
UT = {WOS:001544079300001},
doi = {10.1073/pnas.2422678122},
url = {https://juser.fz-juelich.de/record/1044990},
}