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The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition

AuthorsFranco-Echevarría, E.; González-Polo, Noelia; Zorrilla, Silvia ; Martínez-Lumbreras, Santiago ; Santiveri, Clara M.; Campos-Olivas, Ramón; Sánchez, Mar; Calvo, Olga ; González, Beatriz ; Pérez-Cañadillas, José Manuel
Issue Date2017
PublisherOxford University Press
CitationNucleic Acids Research 45(17): 10293-10305 (2017)
AbstractTranscription 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.
Publisher version (URL)https://doi.org/10.1093/nar/gkx685
Identifiersdoi: 10.1093/nar/gkx685
issn: 0305-1048
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