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bioRxiv · 10.1101/2023.12.13.571423

The prefoldin-like protein AtURI exhibits characteristics of instrinsically disordered proteins.

Gomez-Minguez, Y.·Palacios-Abella, A.·Costigliolo-Rojas, C.·Hernandez-Villa, L.·Barber, M.·Urbez, C.·Alabadi, D.
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Abstract

The prefoldin-like protein UNCONVENTIONAL PREFOLDIN RPB5 INTERACTOR (URI) participates in diverse cellular functions, including protein homeostasis, transcription, translation, and signal transduction. Thus, URI is a highly versatile protein, although the molecular basis of this versatility remains unknown. In this work, we show that Arabidopsis thaliana (Arabidopsis) URI (AtURI) possesses a large intrinsically disordered region (IDR) spanning most of the C-terminal part of the protein, a feature conserved in yeast and human orthologs. Our findings reveal two key characteristics of disordered proteins in AtURI: promiscuity in interacting with partners and protein instability. We propose that these two features contribute to providing AtURI with functional versatility.

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Gomez-Minguez, Y., Palacios-Abella, A., Costigliolo-Rojas, C., Hernandez-Villa, L., Barber, M., Urbez, C., Alabadi, D.. 2023-12-14. The prefoldin-like protein AtURI exhibits characteristics of instrinsically disordered proteins.. https://doi.org/10.1101/2023.12.13.571423

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