ArticleThe Plant cell2016
The Reverse Transcriptase/RNA Maturase Protein MatR Is Required for the Splicing of Various Group II Introns in Brassicaceae Mitochondria.
Article in The Plant cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52 citing papers in PubMed, 106 citations in OpenAlex.
- Evolutionary dynamics and phylogenetic analysis of the mitochondrial genome of the medicinal plant Peucedanum praeruptorum.BMC plant biology · 2026Article
- Assembly and comparative analysis of the first complete mitochondrial genome ofFrontiers in plant science · 2026Article
- Characterization of the complete mitochondrial genome ofFrontiers in plant science · 2026Article
- Structural divergence and molecular adaptation ofFrontiers in plant science · 2026Article
- A record-setting mitogenome in the holoparasitic plant Balanophora yakushimensis accompanied by exceptional loss of organellar DNA repair and recombination genes.BMC biology · 2025Article
- Plant mitochondrial PORR proteins facilitate group II intron splicing by binding to distinct regions within their target introns.Nucleic acids research · 2025Article
- Targeted introduction of premature stop codon in plant mitochondrial mRNA by a designer pentatricopeptide repeat protein with C-to-U editing function.The Plant journal : for cell and molecular biology · 2025Article
- Seeing the unseen in characterizing RNA editome during rice endosperm development.Communications biology · 2024Article
- Temperature-sensitive splicing defects in Arabidopsis mitochondria caused by mutations in the ROOT PRIMORDIUM DEFECTIVE 1 gene.Nucleic acids research · 2024Article
- Mitochondrial atp1 mRNA knockdown by a custom-designed pentatricopeptide repeat protein alters ATP synthase.Plant physiology · 2024Article
- Importance of pre-mRNA splicing and its study tools in plants.Advanced biotechnology · 2024Review
- Review
- Mitochondrial transport of catalytic RNAs and targeting of the organellar transcriptome in human cells.Journal of molecular cell biology · 2024Article
- Mitochondrial RNA maturation.RNA biology · 2024Review
- Comparative Analysis ofBiology · 2023Article
- Genome Editing and Improvement of Abiotic Stress Tolerance in Crop Plants.Life (Basel, Switzerland) · 2023Review
- Comparative analysis of the organelle genomes of three Rhodiola species provide insights into their structural dynamics and sequence divergences.BMC plant biology · 2023Article
- Organellar transcripts dominate the cellular mRNA pool across plants of varying ploidy levels.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
14 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Group II introns are large catalytic RNAs that are ancestrally related to nuclear spliceosomal introns. Sequences corresponding to group II RNAs are found in many prokaryotes and are particularly prevalent within plants organellar genomes. Proteins encoded within the introns themselves (maturases) facilitate the splicing of their own host pre-RNAs. Mitochondrial introns in plants have diverged considerably in sequence and have lost their maturases. In angiosperms, only a single maturase has been retained in the mitochondrial DNA: the matR gene found within NADH dehydrogenase 1 (nad1) intron 4. Its conservation across land plants and RNA editing events, which restore conserved amino acids, indicates that matR encodes a functional protein. However, the biological role of MatR remains unclear. Here, we performed an in vivo investigation of the roles of MatR in Brassicaceae. Directed knockdown of matR expression via synthetically designed ribozymes altered the processing of various introns, including nad1 i4. Pull-down experiments further indicated that MatR is associated with nad1 i4 and several other intron-containing pre-mRNAs. MatR may thus represent an intermediate link in the gradual evolutionary transition from the intron-specific maturases in bacteria into their versatile spliceosomal descendants in the nucleus. The similarity between maturases and the core spliceosomal Prp8 protein further supports this intriguing theory.
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