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- W2912246560 abstract "The prominence of intrinsically disordered proteins (IDPs) in regulatory roles is in no small part due to their flexibility, which allows them to interact with many partners and be accessible to modifying enzymes. The repertoire of IDPs interactions has recently been expanded by our discovery and characterization of the first case of an IDP-IDP high-affinity interaction between the linker histone H1.0 and prothymosin-α (ProTα). Mapping these interactions is an inherently difficult task due to their transient nature, but thanks to single-molecule FRET (smFRET), NMR and molecular simulations, we demonstrated that disorder of the interacting proteins is fully maintained in the complex, where the constituent proteins dynamically interconvert within a broad conformational ensemble with no preferential binding sites. We have now investigated the interaction between the highly acidic ProTα and its basic partner NUPR1: both IDPs are involved in cancer progression, apoptosis, and, like H1.0, in chromatin remodeling. Multiple intra- and inter-molecular distances measured with smFRET show a progressive addition of NUPR1 molecules on a single ProTα chain, which is consistent with results from dual-focus FCS showing a continuous increase in hydrodynamic radius upon titration of ProTα with NUPR1. Using FRET we were able to determine a 10:1 stoichiometric ratio in saturating conditions, which is highly unusual for proteins of roughly similar sizes. However, strikingly, far-UV circular dichroism spectroscopy shows no gain of structure upon formation of this large polyprotein complex, as in the case of ProTα-H1. A pattern is emerging that chromatin-remodeling complexes must be kept amenable of fine-tuning for optimal regulation. Additionally, both ProTα-H1 and ProTα-NUPR1 undergo liquid-liquid phase transition in the micromolar concentration range, suggesting that disorder, valency and accessibility of these complexes might also be important to grant a further level of regulation via phase transition." @default.
- W2912246560 created "2019-02-21" @default.
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- W2912246560 date "2019-02-01" @default.
- W2912246560 modified "2023-10-06" @default.
- W2912246560 title "Highly Disordered 10:1 Complex of Two Anti-Apoptotic, Chromatin-Remodelling Intrinsically Disordered Proteins" @default.
- W2912246560 doi "https://doi.org/10.1016/j.bpj.2018.11.2445" @default.
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