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Trigger factor chaperone acts as a mechanical foldase
, R. Tapia-Rojo, E.C. Eckels, J. Valle-Orero, J.M. Fernandez
Published in Nature Publishing Group
PMID: 28939815
Volume: 8
Issue: 1
Proteins fold under mechanical forces in a number of biological processes, ranging from muscle contraction to co-translational folding. As force hinders the folding transition, chaperones must play a role in this scenario, although their influence on protein folding under force has not been directly monitored yet. Here, we introduce single-molecule magnetic tweezers to study the folding dynamics of protein L in presence of the prototypical molecular chaperone trigger factor over the range of physiological forces (4-10 pN). Our results show that trigger factor increases prominently the probability of folding against force and accelerates the refolding kinetics. Moreover, we find that trigger factor catalyzes the folding reaction in a force-dependent manner; as the force increases, higher concentrations of trigger factor are needed to rescue folding. We propose that chaperones such as trigger factor can work as foldases under force, a mechanism which could be of relevance for several physiological processes. © 2017 The Author(s).
About the journal
JournalNature Communications
PublisherNature Publishing Group