Abstract
Serine/arginine-rich (SR) proteins play important roles in constitutive and alternative splicing and other aspects of mRNA metabolism. We have previously isolated a unique plant SR protein (SR45) with atypical domain organization. However, the biological and molecular functions of this novel SR protein are not known. Here, we report biological and molecular functions of this protein. Using an in vitro splicing complementation assay, we showed that SR45 functions as an essential splicing factor. Furthermore, the alternative splicing pattern of transcripts of several other SR genes was altered in a mutant, sr45-1, suggesting that the observed phenotypic abnormalities in sr45-1 are likely due to altered levels of SR protein isoforms, which in turn modulate splicing of other pre-mRNAs. sr45-1 exhibited developmental abnormalities, including delayed flowering, narrow leaves and altered number of petals and stamens. The late flowering phenotype was observed under both long days and short days and was rescued by vernalization. FLC, a key flowering repressor, is up-regulated in sr45-1 demonstrating that SR45 influences the autonomous flowering pathway. Changes in the alternative splicing of SR genes and the phenotypic defects in the mutant were rescued by SR45 cDNA, further confirming that the observed defects in the mutant are due to the lack of SR45. These results indicate that SR45 is a novel plant-specific splicing factor that plays a crucial role in regulating developmental processes.
Highlights
SR proteins constitute a highly conserved family of structurally and functionally related non-snRNP proteins with multiple roles in pre-mRNA splicing and other aspects of RNA metabolism [1,2,3,4,5]
To identify Arabidopsis SR45 homologs in other organism we searched all the available plant, fungal and animal genomes and EST sequence databases. These searches revealed the presence of SR45 in rice, maize and in many other flowering plants, but not in algae (Chlamydomonas reinhardtii; Cyanidioschyzon merolae), a diatom (Thalassiosira pseudonana) and animals. These results indicate that SR45 has appeared later in evolution only in the flowering plants clade
The absence of SR45 in animals and algae and its presence in flowering plants suggest that SR45 may have evolved to perform functions that are specific to flowering plants
Summary
SR proteins constitute a highly conserved family of structurally and functionally related non-snRNP proteins with multiple roles in pre-mRNA splicing and other aspects of RNA metabolism [1,2,3,4,5]. These proteins have a modular domain structure with one or two N-terminal RNA recognition motifs (RRMs) and a C-terminal arginine/serine-rich (RS) domain. Some animal SR proteins that shuttle between the nucleus and cytoplasm function in mRNA export, mRNA stability and/or translation [1] These studies underscore the importance of this family of proteins in RNA metabolism. SR proteins show functional redundancy in in vitro splicing assays, in vivo studies with non-plant systems indicate that some SR proteins are redundant whereas others are not [4]
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