Noelia González-Polo
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Noelia González-Polo has a total of 9 co-authors. Here are the top co-authors by number of shared publications:
- Beatriz González
Department of Crystallography and Structural Biology, Institute of Physical-Chemistry Blas Cabrera, CSIC, Serrano 119, 28006 Madrid, Spain
1 shared publication - Clara M. Santiveri
Spectroscopy and Nuclear Magnetic Resonance Unit, Spanish National Cancer Research Centre (CNIO), Madrid, Spain
1 shared publication - Elsa Franco-Echevarría
MRC Laboratory of Molecular Biology, Cambridge, UK
1 shared publication - José Manuel Pérez-Cañadillas
Department of Biological Physical Chemistry, Institute of Physical-Chemistry “Rocasolano”, CSIC, C/ Serrano 119, 28006 Madrid, Spain
1 shared publication - Mar Sánchez
Instituto de Biología Funcional y Genómica (IBFG), CSIC/Universidad de Salamanca, Salamanca, Spain
1 shared publication - Olga Calvo
Instituto de Biología Funcional y Genómica, Consejo Superior de Investigaciones Científicas, Universidad de Salamanca, Salamanca, Spain
1 shared publication
Latest Publications
- Open Access
- 31 July 2017
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 45 (17) , 10293-10305
The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition
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.
- 31 July 2017
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 45 (17) , 10293-10305
Open AccessThe structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition
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.