We are studying how protein folding can occur while chaperone bound and are using folding biosensors to discover a wealth of new chaperones
Wu K, Minshull TC, Radford SE, Calabrese AN, Bardwell JCA. Trigger factor both holds and folds its client proteins. Nat Commun. 2022 Jul 15;13(1):4126. doi: 10.1038/s41467-022-31767-6. PubMed
Mitra R, Gadkari VV, Meinen BA, van Mierlo CPM, Ruotolo BT, Bardwell JCA. Mechanism of the small ATP-independent chaperone Spy is substrate specific. Nat Commun. 2021 Feb 8;12(1):851. doi: 10.1038/s41467-021-21120-8. PubMed
Lee C, Betschinger P, Wu K, Zyla DS, Glockshuber R, Bardwell JCA. A metabolite binding protein moonlights as a bile-responsive chaperone. EMBO J. 2020 Sep 3;e104231. doi: 10.15252/embj.2019104231. Online ahead of print. PubMed
Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol. 2011 18(3):262-9. PubMed This paper was the subject of a “News and Views” [PDF] citation in Nature by Evan T. Powers and Willian E. Balch.