The structure and selectivity of the SR protein SRSF2 RRM domain with RNA.

Phelan, Marie M and Goult, Benjamin T and Clayton, Jonathan C and Hautbergue, Guillaume M and Wilson, Stuart A and Lian, Lu-Yun (2012) The structure and selectivity of the SR protein SRSF2 RRM domain with RNA. Nucleic acids research, 40 (7). pp. 3232-3244. ISSN 1362-4962. E-ISSN 1362-4962. (doi:https://doi.org/10.1093/nar/gkr1164) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1093/nar/gkr1164

Abstract

SRSF2 is a prototypical SR protein which plays important roles in the alternative splicing of pre-mRNA. It has been shown to be involved in regulatory pathways for maintaining genomic stability and play important roles in regulating key receptors in the heart. We report here the solution structure of the RNA recognition motifs (RRM) domain of free human SRSF2 (residues 9-101). Compared with other members of the SR protein family, SRSF2 structure has a longer L3 loop region. The conserved aromatic residue in the RNP2 motif is absent in SRSF2. Calorimetric titration shows that the RNA sequence 5'AGCAGAGUA3' binds SRSF2 with a K(d) of 61 ± 1 nM and a 1:1 stoichiometry. NMR and mutagenesis experiments reveal that for SFSF2, the canonical β1 and β3 interactions are themselves not sufficient for effective RNA binding; the additional loop L3 is crucial for RNA complex formation. A comparison is made between the structures of SRSF2-RNA complex with other known RNA complexes of SR proteins. We conclude that interactions involving the L3 loop, N- and C-termini of the RRM domain are collectively important for determining selectivity between the protein and RNA.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Ben Goult
Date Deposited: 07 Aug 2014 16:07 UTC
Last Modified: 06 May 2015 11:15 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42116 (The current URI for this page, for reference purposes)
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