Roquin exhibits opposing effects on RNA stem-loop stability through its two ROQ domain binding sites.

ABSTRACT: The interaction of mRNA and regulatory proteins is critical for posttranscriptional control. For proper function, these interactions, as well as the involved protein and RNA structures, are highly dynamic, and thus, mechanistic insights from structural biology are challenging to obtain. In this study, we employ a multifaceted approach combining single-molecule force spectroscopy (SMFS) with NMR spectroscopy to analyze the concerted interaction of the two RNA-binding interfaces (A-site and B-site) of the immunoregulatory protein Roquin's ROQ domain with the 3' untranslated region (UTR) of the Ox40 mRNA. This 3'UTR contains two specific hairpin structures termed constitutive and alternative decay elements (CDE, ADE), which mediate mRNA degradation through Roquin binding. Our single-mo

SUBMITTER: Tants JN 

PROVIDER: S-EPMC12012478 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature