Abstract
In land plants, the pentatricopeptide repeat (PPR) proteins form a large family involved in post-transcriptional processing of RNA in mitochondria and chloroplasts, which is critical for plant development and evolutionary adaption. Although studies showed a number of PPR proteins generally influence the editing of organellar genes, few of them were characterized in detail in rice. Here, we report a PLS-E subclass PPR protein in rice, PPR756, loss of function of which led to the abolishment of RNA editing events among three mitochondrial genes including atp6, ccmC, and nad7. Their defective C-to-U transformation then resulted in improper amino acid retention which could cause abortive pollen development. Furthermore, PPR756 could bind to the three target genes directly and interact with three OsMORFs (multiple organellar RNA editing factors): OsMORF1, OsMORF8-1, and OsMORF8-2. The knock-out plants of PPR756 exhibited retarded growth and greener leaves during the early vegetative stages, along with sterile pollen and lower seed setting at the reproductive stage. These results established a role for PPR756 in rice development, participating in RNA editing of three various transcripts and cooperating with OsMORFs via an editosome manner in rice.
Highlights
The pentatricopeptide repeat (PPR) proteins constitute an interesting protein family widely spread in eukaryotes, from algae to humans, their numbers vary considerably in different organisms (Lurin et al, 2004)
Since Os12g19260 encodes a PPR protein with 756 amino acids, we identified it as PPR756 in this study
In order to explore the function of PPR756 in detail, we generated over-expression (OE) transgenic lines, in which the CDS of PPR756 was driven by the ubiquitin promoter and fused with the Flag and cMyc tags (Supplementary Figure S2B)
Summary
The pentatricopeptide repeat (PPR) proteins constitute an interesting protein family widely spread in eukaryotes, from algae to humans, their numbers vary considerably in different organisms (Lurin et al, 2004). This protein family has been suggested to have undergone great expansion when the terrestrial plants came into being andrange from ∼100 Based on the alignment of multiple linear sequence, many distinct PPR motifs definitions were developed, including differing motif borders and numbering schemes (Barkan et al, 2012; Yagi et al, 2013; Yin et al, 2013). Recent study suggested the definition based on the analysis of protein structures could be more accurate (Cheng et al, 2016)
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
