2026-06-16T14:05:43Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/71052024-11-29T15:24:32Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597
Repisalud
author
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
funder
Ministerio de Economía y Competitividad (España)
2019-02-05T10:19:12Z
2019-02-05T10:19:12Z
2017-09-29
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
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.
eng
The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition
journal article
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Thestructureoftranscription_2017.pdf.txt
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