The prefoldin ‐like protein AtURI exhibits characteristics of intrinsically disordered proteins
The prefoldin-like protein AtURI has a large, disordered region (colored red) at the C-terminus of the structured prefoldin domain (colored blue) that confers AtURI promiscuity for protein –protein interactions and instability to allow tight control of AtURI levels. 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 thatArabidopsis 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.
Source: FEBS Letters - Category: Biochemistry Authors: Yaiza G ómez‐Mínguez,
Alberto Palacios‐Abella,
Cecilia Costigliolo‐Rojas,
Mariana Barber,
Laura Hernández‐Villa,
Cristina Úrbez,
David Alabadí Tags: Research Article Source Type: research
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