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Título: | The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition |
Autor: | Franco-Echevarría, E. CSIC ORCID; González-Polo, Noelia CSIC ORCID; Zorrilla, Silvia CSIC ORCID ; Martínez-Lumbreras, Santiago CSIC ORCID; Santiveri, Clara M. CSIC ORCID; Campos-Olivas, Ramón CSIC ORCID; Sánchez, Mar CSIC; Calvo, Olga CSIC ORCID; González, Beatriz CSIC ORCID; Pérez Cañadillas, José Manuel CSIC ORCID | Fecha de publicación: | 2017 | Editor: | Oxford University Press | Citación: | Nucleic Acids Research 45(17): 10293-10305 (2017) | Resumen: | Transcription termination of non-coding RNAs is regulated in yeast by a complex of three RNA binding proteins: Nrd1, Nab3 and Sen1. Nrd1 is central in this process by interacting with Rbp1 of RNA polymerase II, Trf4 of TRAMP and GUAA/G terminator sequences. We lack structural data for the last of these binding events. We determined the structures of Nrd1 RNA binding domain and its complexes with three GUAA-containing RNAs, characterized RNA binding energetics and tested rationally designed mutants in vivo. The Nrd1 structure shows an RRM domain fused with a second α/β domain that we name split domain (SD), because it is formed by two non-consecutive segments at each side of the RRM. The GUAA interacts with both domains and with a pocket of water molecules, trapped between the two stacking adenines and the SD. Comprehensive binding studies demonstrate for the first time that Nrd1 has a slight preference for GUAA over GUAG and genetic and functional studies suggest that Nrd1 RNA binding domain might play further roles in non-coding RNAs transcription termination. | Versión del editor: | https://doi.org/10.1093/nar/gkx685 | URI: | http://hdl.handle.net/10261/162591 | DOI: | 10.1093/nar/gkx685 | Identificadores: | doi: 10.1093/nar/gkx685 issn: 0305-1048 |
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