| Autor: |
Gómez‐Mínguez, Yaiza, Palacios‐Abella, Alberto, Costigliolo‐Rojas, Cecilia, Barber, Mariana, Hernández‐Villa, Laura, Úrbez, Cristina, Alabadí, David |
| Předmět: |
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| Zdroj: |
FEBS Letters; Mar2024, Vol. 598 Issue 5, p556-570, 15p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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