A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A
Abstract Eukaryotic translation elongation factor 1A (eEF1A) is a highly abundant, multi-domain GTPase. Post-translational steps essential for eEF1A biogenesis are carried out by bespoke chaperones but co-translational mechanisms tailored to eEF1A folding remain unexplored. Here, we use AlphaPulldow...
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Main Authors: | Ibrahim M. Sabbarini, Dvir Reif, Kibum Park, Alexander J. McQuown, Anjali R. Nelliat, Charlotte Trejtnar, Volker Dötsch, Eugene I. Shakhnovich, Andrew W. Murray, Vladimir Denic |
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Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2025-02-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-025-56489-3 |
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