2026-06-14T03:29:05Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/71052024-11-29T15:24:32Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597

00925njm 22002777a 4500 dc Franco-Echevarría, Elsa author González-Polo, Noelia author Zorrilla, Silvia author Martínez-Lumbreras, Santiago author Santiveri, Clara M author Campos Olivas, Ramon author Sánchez, Mar author Calvo, Olga author González, Beatriz author Pérez-Cañadillas, José Manuel author 2017-09-29 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. Nucleic Acids Res. 2017 ;45(17):10293-10305. 10.1093/nar/gkx685 1362-4962 0305-1048 Nucleic acids research 28973465 http://hdl.handle.net/20.500.12105/7105 The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition