1. Structure-Dependent Binding of hnRNPA1 to Telomere RNA
- Author
-
Xiao Liu, Yan Xu, Hong-Liang Bao, Danzhou Yang, Kei Wada, Yuma Takeda, Takumi Ishizuka, Kazuo Nagasawa, and Keisuke Iida
- Subjects
0301 basic medicine ,Magnetic Resonance Spectroscopy ,Photochemistry ,Fluorescent Antibody Technique ,RNA-dependent RNA polymerase ,010402 general chemistry ,Models, Biological ,01 natural sciences ,Biochemistry ,Article ,Catalysis ,Substrate Specificity ,Small Molecule Libraries ,Structure-Activity Relationship ,03 medical and health sciences ,Colloid and Surface Chemistry ,Humans ,Telomerase ,Telomere-binding protein ,Molecular Structure ,Chemistry ,Intron ,RNA ,General Chemistry ,Non-coding RNA ,Molecular biology ,0104 chemical sciences ,Cell biology ,G-Quadruplexes ,RNA silencing ,Cross-Linking Reagents ,030104 developmental biology ,Microscopy, Fluorescence ,RNA editing ,Small nuclear RNA ,HeLa Cells ,Protein Binding - Abstract
Telomeric repeat-containing RNA is a new noncoding RNA molecule that performs various biofunctions. Heterogeneous nuclear ribonucleoprotein (hnRNP) A1 is an RNA-binding protein involved in the telomere maintenance machinery. To date, little is known about how hnRNPA1 binds to telomeric RNA. In this study, we investigated the binding affinity and recognition mechanism of telomere RNA with the RNA recognition motif of hnRNPA1. Using the photochemical cross-linking method, we showed that the telomere RNA G-quadruplex with loops is important in the interaction of telomere RNA with hnRNPA1. Using small-molecule probes, we directly visualized the complex formed by the telomere RNA G-quadruplex and hnRNPA1 in vitro and in live cells. The results suggested that the structure-dependent binding of hnRNPA1 to telomere RNA regulates the telomere function. Therefore, our study provides new insights into the interactions between the RNA G-quadruplex and proteins at the telomere.
- Published
- 2017