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Nucleic Acids Res. 2016 Jan 8;44(1):437-48. doi: 10.1093/nar/gkv1303. Epub 2015 Nov 23.

Gbp2 interacts with THO/TREX through a novel type of RRM domain.

Author information

1
Department of Biological Physical Chemistry, Instituto de Química-Física 'Rocasolano', CSIC, Serrano-119, 28006 Madrid, Spain.
2
Equipe Labellisée La Ligue, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGMBC), Centre National de Recherche Scientifique (CNRS) UMR 7104/Institut National de Santé et de Recherche Médicale (INSERM) U964/Université de Strasbourg, 67404 Illkirch, France.
3
Department of Cellular and Molecular Biology, Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
4
Equipe Labellisée La Ligue, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGMBC), Centre National de Recherche Scientifique (CNRS) UMR 7104/Institut National de Santé et de Recherche Médicale (INSERM) U964/Université de Strasbourg, 67404 Illkirch, France seraphin@igbmc.fr.
5
Department of Biological Physical Chemistry, Instituto de Química-Física 'Rocasolano', CSIC, Serrano-119, 28006 Madrid, Spain jmperez@iqfr.csic.es.

Abstract

Metazoan SR and SR-like proteins are important regulatory factors in RNA splicing, export, translation and RNA decay. We determined the NMR structures and nucleic acid interaction modes of Gbp2 and Hrb1, two paralogous budding yeast proteins with similarities to mammalian SR proteins. Gbp2 RRM1 and RRM2 recognise preferentially RNAs containing the core motif GGUG. Sequence selectivity resides in a non-canonical interface in RRM2 that is highly related to the SRSF1 pseudoRRM. The atypical Gbp2/Hrb1 C-terminal RRM domains (RRM3) do not interact with RNA/DNA, likely because of their novel N-terminal extensions that block the canonical RNA binding interface. Instead, we discovered that RRM3 is crucial for interaction with the THO/TREX complex and identified key residues essential for this interaction. Moreover, Gbp2 interacts genetically with Tho2 as the double deletion shows a synthetic phenotype and preventing Gbp2 interaction with the THO/TREX complex partly supresses gene expression defect associated with inactivation of the latter complex. These findings provide structural and functional insights into the contribution of SR-like proteins in the post-transcriptional control of gene expression.

PMID:
26602689
PMCID:
PMC4705658
DOI:
10.1093/nar/gkv1303
[Indexed for MEDLINE]
Free PMC Article

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