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Review
. 2015 Jul 24;5(3):1717-40.
doi: 10.3390/biom5031717.

Pre-mRNA Splicing in Plants: In Vivo Functions of RNA-Binding Proteins Implicated in the Splicing Process

Katja Meyer  1 , Tino Koester  2 , Dorothee Staiger  3
Affiliations
Review

Pre-mRNA Splicing in Plants: In Vivo Functions of RNA-Binding Proteins Implicated in the Splicing Process

Katja Meyer et al. Biomolecules. .

Abstract

Alternative pre-messenger RNA splicing in higher plants emerges as an important layer of regulation upon exposure to exogenous and endogenous cues. Accordingly, mutants defective in RNA-binding proteins predicted to function in the splicing process show severe phenotypic alterations. Among those are developmental defects, impaired responses to pathogen threat or abiotic stress factors, and misregulation of the circadian timing system. A suite of splicing factors has been identified in the model plant Arabidopsis thaliana. Here we summarize recent insights on how defects in these splicing factors impair plant performance.

Keywords: Arabidopsis; RNA-binding protein; splicing.

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Figures

Figure 1
Figure 1
Splicing signals involved in pre-mRNA splicing. Introns are delineated by short consensus sequences, the 5' and 3' splice sites (R = Purine, A/G), the polypyrimidine tract (Y = Pyrimidine, C/T), and the branch point sequence. Intronic splicing silencers (ISS), intronic splicing enhancers (ISE), exonic splicing silencers (ESS), and exonic splicing enhancers (ESE) are additional sequence elements serving as docking sites for protein factors that promote or impair assembly of the spliceosome at particular splice sites and thus control the splicing process. The green boxes denote exons. Introns are represented by lines with the consensus sequences indicated (see text for details).
Figure 2
Figure 2
The spliceosomal cycle. The splicing process is initiated by the interaction of the U1 snRNP with the 5' splice site through base pairing of the U1 snRNA to complementary sequences. The U2AF subunit U2AF35 binds to the intron/exon border and the subunit U2AF65 binds to the polypyrimidine tract upstream of the intron/exon border, leading to the complex E. Subsequently, the U2 snRNP binds to the branch point, defining complex A. The U4/U6.U5 snRNP is then docked onto the U2 snRNP, leading to the precatalytic complex B. After major rearrangements and the release of the U1 and U4 snRNPs, the activated complex Bact is generated. In the first step of the splicing reaction, the pre-mRNA is cleaved at the 5' splice site and lariat formation of the intron sequence takes place by ligating its 5' end to the branch point adenosine. This leads to the formation of complex C that then catalyzes the second step of the splicing reaction, the cleavage at the 3' splice site, the ligation of the exons, and the release of the spliced mRNA. The lariat is degraded and the snRNPs are recycled. The proteins with a demonstrated role in pre-mRNA splicing in Arabidopsis are shown where in the spliceosomal cycle they are proposed to act, based on the homology to their human counterparts. The boxes denote exons; the thin line denotes the intron. NTC, Nineteen Complex.
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