Journal Article

FZJ-2025-03475

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Trigger factor accelerates nascent chain compaction and folding

Till, K. (Corresponding author) ; Seinen, A.-B. ; Wruck, F. ; Sunderlikova, V. ; Galmozzi, C. V. ; Katranidis, A.FZJ* ; Bukau, B. ; Kramer, G. ; Tans, S. J.

2025
National Acad. of Sciences Washington, DC

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Please use a persistent id in citations: doi:10.1073/pnas.2422678122  doi:10.34734/FZJ-2025-03475

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.

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Contributing Institute(s):

1. Strukturbiologie (ER-C-3)

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 2025

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