Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1

• Published in: Nucleic acids research Vol. 49; no. 5; pp. 2403 - 2417
• Main Authors: Loughlin, Fionna E, West, Danella L, Gunzburg, Menachem J, Waris, Saboora, Crawford, Simon A, Wilce, Matthew C J, Wilce, Jacqueline A
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 18.03.2021
• Subjects: 3' Untranslated Regions; Amyloid - ultrastructure; Binding Sites; DNA - chemistry; DNA - metabolism; Humans; Models, Molecular; NAR Breakthrough; Oligonucleotides - chemistry; Oligonucleotides - metabolism; Protein Conformation; RNA - chemistry; RNA - metabolism; T-Cell Intracellular Antigen-1 - chemistry; T-Cell Intracellular Antigen-1 - metabolism; T-Cell Intracellular Antigen-1 - ultrastructure; Tumor Suppressor Protein p53 - genetics; Tumor Suppressor Protein p53 - metabolism

Abstract TIA-1 is an RNA-binding protein that sequesters target RNA into stress granules under conditions of cellular stress. Promotion of stress granule formation by TIA-1 depends upon self-association of its prion-like domain that facilitates liquid-liquid phase separation and is thought to be enh...