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

Autor: Gómez-Mínguez Y; Instituto de Biología Molecular y Celular de Plantas (CSIC-UPV), Valencia, Spain., Palacios-Abella A; Instituto de Biología Molecular y Celular de Plantas (CSIC-UPV), Valencia, Spain., Costigliolo-Rojas C; Instituto de Biología Molecular y Celular de Plantas (CSIC-UPV), Valencia, Spain., Barber M; Fundación Instituto Leloir, Buenos Aires, Argentina., Hernández-Villa L; Instituto de Biología Molecular y Celular de Plantas (CSIC-UPV), Valencia, Spain., Úrbez C; Instituto de Biología Molecular y Celular de Plantas (CSIC-UPV), Valencia, Spain., Alabadí D; Instituto de Biología Molecular y Celular de Plantas (CSIC-UPV), Valencia, Spain.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2024 Mar; Vol. 598 (5), pp. 556-570. Date of Electronic Publication: 2024 Feb 01.
DOI: 10.1002/1873-3468.14811
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.
(© 2024 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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