Evidence map›Paper›PMID 19238562›Full record

ArticlePlant molecular biology2009

Plant-specific SR-related protein atSR45a interacts with spliceosomal proteins in plant nucleus.

Noriaki Tanabe, Ayako Kimura, Kazuya Yoshimura, Shigeru Shigeoka

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Article in Plant molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

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0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

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  20. Unraveling the circadian clock in Arabidopsis.Plant signaling & behavior · 2013
    Article
4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Noriaki TanabeDepartment of Advanced Bioscience, Faculty of Agriculture, Kinki University, Nakamachi, Nara, Japan.
Ayako Kimura
Kazuya Yoshimura
Shigeru Shigeoka

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serine/arginine-rich (SR) protein and its homologues (SR-related proteins) are important regulators of constitutive and/or alternative splicing and other aspects of mRNA metabolism. To clarify the contribution of a plant-specific and stress-responsive SR-related protein, atSR45a, to splicing events, here we analyzed the interaction of atSR45a with the other splicing factors by conducting a yeast two-hybrid assay and a bimolecular fluorescence complementation analysis. The atSR45a-1a and -2 proteins, the presumed mature forms produced by alternative splicing of atSR45a, interacted with U1-70K and U2AF(35)b, splicing factors for the initial definition of 5' and 3' splice sites, respectively, in the early stage of spliceosome assembly. Both proteins also interacted with themselves, other SR proteins (atSR45 and atSCL28), and PRP38-like protein, a homologue of the splicing factor essential for cleavage of the 5' splice site. The mapping of deletion mutants of atSR45a proteins revealed that the C-terminal arginine/serine-rich (RS) domain of atSR45a proteins are required for the interaction with U1-70K, U2AF(35)b, atSR45, atSCL28, PRP38-like protein, and themselves, and the N-terminal RS domain enhances the interaction efficiency. Interestingly, the distinctive N-terminal extension in atSR45a-1a protein, but not atSR45a-2 protein, inhibited the interaction with these splicing factors. These findings suggest that the atSR45a proteins help to form the bridge between 5' and 3' splice sites in the spliceosome assembly and the efficiency of spliceosome formation is affected by the expression ratio of atSR45a-1a and atSR45a-2.

Indexed as

Alternative SplicingArabidopsisArabidopsis ProteinsCarrier ProteinsCell NucleusDNA-Binding ProteinsGene LibraryProtein BindingRNA-Binding ProteinsRNA, MessengerRNA, PlantRNA Splice SitesSpliceosomesSplicing Factor U2AFTwo-Hybrid System TechniquesArabidopsis ProteinsCarrier ProteinsDNA-Binding ProteinsRNA-Binding ProteinsRNA, MessengerRNA, PlantRNA Splice SitesSplicing Factor U2AFSR45 protein, ArabidopsisU2AF(35)b protein, Arabidopsis

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.