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PreprintCited by 17RNA Research and SplicingPlant Molecular Biology ResearchPhotosynthetic Processes and Mechanisms

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The Arabidopsis SR45 splicing factor bridges the splicing machinery and the exon-exon junction complex

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Fanara, Steven, Schloesser, Marie, Joris, Marine, De Franco, Simona, Vandevenne, Marylène, Kerff, Frédéric, Hanikenne, Marc, Motte, Patrick·2023·Journal of Experimental Botany
DOI 10.1101/2023.08.07.552250

Preprint — published as 10.1093/jxb/erae002

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Abstract

The Arabidopsis splicing factor serine/arginine-rich 45 (SR45) contributes to several biological processes. The sr45-1 loss-of-function mutant exhibits delayed root development, late flowering, unusual numbers of floral organs, shorter siliques with decreased seed sets, narrower leaves and petals, and altered metal distribution. SR45 bears a unique RNA recognition motif (RRM) flanked by one serine/arginine-rich (RS) domain on both sides. Here, we studied the function of each of SR45 domains by examining their involvement in: (i) the spatial distribution of SR45, (ii) the establishment of a protein-protein interaction network including spliceosomal and exon-exon junction complex (EJC) components, and (iii) the RNA binding specificity. We report that the endogenous SR45 promoter is active during vegetative and reproductive growth, and that the SR45 protein localizes in the nucleus. We demonstrate that the C-terminal arginine/serine-rich domain is a determinant of nuclear localization. We show that the SR45 RNA recognition motif (RRM) domain specifically binds purine-rich RNA motifs via three residues (H101, H141, Y143), and is also involved in protein-protein interactions. We further show that SR45 bridges both mRNA splicing and surveillance machineries as a partner of EJC core components and peripheral factors, which requires phosphoresidues likely phosphorylated by kinases from both CLK and SRPK families. Our findings provide insights into the contribution of each SR45 domain to both spliceosome and EJC assemblies. Highlight: The contribution of the Arabidopsis SR45 splicing factor individual domains to its nuclear localization, ability to contact in planta novel protein partners and specifically bind RNA motifs was examined.

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Metadata

Authors
Fanara, S., Schloesser, M., Joris, M., De Franco, S., Vandevenne, M., Kerff, F., Hanikenne, M., & Motte, P.
Affiliations
University of Liège (BE)
Corresponding author
Fanara, Steven
ORCID
Venue
Journal of Experimental Botany
Publisher
openRxiv
Published
2023-08-07
Volume
75
Issue
8
Pages
2280-2298
ISSN
0022-0957 (ISSN-L)
DOI
10.1101/2023.08.07.552250
OpenAlex
W4390607216
Cited by
17
References
1
Citations by year
2026: 8 · 2025: 6 · 2024: 3
FWCI
2.31
Type
journal article
Language
en
Open access
Licence
cc-by-nc-nd
Locations
  • Journal of Experimental Botany (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • ORBi (University of Liège) (submittedVersion, cc-by-nc-nd)
Funders
  • Fonds De La Recherche Scientifique - FNRS (PDR T0120.18, PDR-T.0206.13, J.0082.21, T0120.18, J.0009.17)
  • Fonds pour la Formation à la Recherche dans l’Industrie et dans l’Agriculture
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
Keywords
SR proteins, RNA recognition motif, RS domain, nuclear localization, RNA binding specificity, protein-protein interaction, spliceosome assembly, RNA surveillance, Arabidopsis thaliana, root development, flowering time, floral organ number, seed set, metal distribution
MeSH terms
RNA Splicing Factors, Arginine, Exons, Humans, RNA Splicing, Serine, RNA-Binding Proteins, Arabidopsis, Arabidopsis Proteins

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