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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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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