4.8 Article

Structure-Dependent Binding of hnRNPA1 to Telomere RNA

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 139, Issue 22, Pages 7533-7539

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b01599

Keywords

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Funding

  1. Kohnan Asia Scholarship Foundation
  2. Nakatani Foundation Scholarship
  3. JSPS KAKENHI [16K17938, 26288083]
  4. Takeda Science Foundation
  5. Grants-in-Aid for Scientific Research [16K17938, 26282214, 17H03091, 16K18908, 16H04754, 16K13094, 26288083] Funding Source: KAKEN

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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.

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