Abstract
Mago nashi (MAGO) and Y14 proteins are highly conserved among eukaryotes. In this study, we identified two MAGO (designated as HbMAGO1 andHbMAGO2) and two Y14 (designated as HbY14aand HbY14b) genes in the rubber tree (Hevea brasiliensis) genome annotation. Multiple amino acid sequence alignments predicted that HbMAGO and HbY14 proteins are structurally similar to homologous proteins from other species. Tissue-specific expression profiles showed that HbMAGO and HbY14 genes were expressed in at least one of the tissues (bark, flower, latex, leaf and root) examined. HbMAGOs and HbY14s were predominately located in the nucleus and were found to interact in yeast two-hybrid analysis (YTH) and bimolecular fluorescence complementation (BiFC) assays. HbMAGOs and HbY14s showed the highest transcription in latex and were regulated by ethylene and jasmonate. Interaction between HbMAGO2 and gp91phox (a large subunit of nicotinamide adenine dinucleotide phosphate) was identified using YTH and BiFC assays. These findings suggested that HbMAGO may be involved in the aggregation of rubber particles in H. brasiliensis.
Highlights
The exon junction complex (EJC) regulates posttranscriptional events that include mRNA intracellular export, cytoplasmic localization, non-sense mediated mRNA decay (NMD) and translation enhancement in metazoans (Park and Muench, 2007; Lee et al, 2009; Ashton-Beaucage et al, 2010; Roignant and Treisman, 2010; Boothby and Wolniak, 2011; Mufarrege et al, 2011)
Our results indicate that HbMAGO may be involved in the aggregation of natural rubber in rubber trees
Since ET and JA have an important role as signaling molecules that regulate rubber biosynthesis in rubber trees (Hao and Wu, 2000; Zeng et al, 2009), we examined whether exposure to ET or JA could influence HbMAGO and HbY14 expression in latex (Figure 4B), despite the lack of evidence relating Mago nashi (MAGO) and Y14s to hormone signaling pathways
Summary
The exon junction complex (EJC) regulates posttranscriptional events that include mRNA intracellular export, cytoplasmic localization, non-sense mediated mRNA decay (NMD) and translation enhancement in metazoans (Park and Muench, 2007; Lee et al, 2009; Ashton-Beaucage et al, 2010; Roignant and Treisman, 2010; Boothby and Wolniak, 2011; Mufarrege et al, 2011). Based on the crystal structures of the Drosophila and human MAGO-Y14 complex, MAGO and Y14 proteins are core components of the EJC and can form a stable heterodimer that strongly associates with spliced mRNA (Lau et al, 2003; Shi and Xu, 2003). Both MAGO and Y14 are evolutionarily highly conserved proteins (Hachet and Ephrussi, 2001; Mohr et al, 2001) and slow co-evolution of the two protein families is required for the maintenance of their obligate heterodimerization mode (Gong et al, 2014). The crystal structure of the heterodimeric complexes, formed in the absence of RNA, shows that the RNAbinding motif is used for Y14/MAGO protein-protein interaction and is not readily available for binding RNA (Fribourg et al, 2003; Lau et al, 2003; Shi and Xu, 2003)
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