Structure-Dependent Binding of hnRNPA1 to Telomere RNA

被引:46
作者
Liu, Xiao [1 ]
Ishizuka, Takumi [1 ]
Bao, Hong-Liang [1 ]
Wada, Kei [2 ]
Takeda, Yuma [1 ]
Iida, Keisuke [3 ]
Nagasawa, Kazuo [3 ]
Yang, Danzhou [4 ]
Xu, Yan [1 ]
机构
[1] Univ Miyazaki, Div Chem, Dept Med Sci, Fac Med, 5200 Kihara, Kiyotake, Miyazaki 8891692, Japan
[2] Univ Miyazaki, Org Promot Tenure Track, 1-1 Gakuenkibanadai Nishi, Kiyotake, Miyazaki 8892192, Japan
[3] Tokyo Univ Agr & Technol, Dept Biotechnol & Life Sci, 2-24-16 Naka Cho, Koganei, Tokyo 1848588, Japan
[4] Purdue Univ, Coll Pharm, Dept Med Chem & Mol Pharmacol, 201 South Univ St, W Lafayette, IN 47907 USA
关键词
REPEAT-CONTAINING RNA; G-QUADRUPLEX STRUCTURE; TERRA; DNA; PROTEIN; LENGTH; CELLS; A1; IDENTIFICATION; TRANSCRIPTION;
D O I
10.1021/jacs.7b01599
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:7533 / 7539
页数:7
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