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Quadrado, M.

Publications and source records attributed to Quadrado, M..

2 recordsLinked to original sources

The radish Ogura fertility restorer impedes translation elongation along its cognate CMS-causing mRNA

The control of mRNA translation has been increasingly recognized as a key regulatory step for gene control but clear examples in eukaryotes are still scarce. Nucleo-cytoplasmic male sterilities (CMS) represent ideal genetic models to dissect genetic interactions between the mitochondria and the nucleus in plants. This trait is determined by specific mitochondrial genes and is associated with a pollen sterility phenotype that can be suppressed by nuclear genes known as restorer-of-fertility (Rf) genes. In the study, we focused on the Ogura CMS system in rapeseed and showed that the suppression to male sterility by the PPR-B fertility restorer (also called Rfo) occurs through a specific inhibition of the translation of the mitochondria-encoded CMS-causing mRNA orf138. We also demonstrate that PPR-B binds within the coding sequence of orf138 and acts as a ribosome blocker to specifically impede translation elongation along the orf138 mRNA. Rfo is the first recognized fertility restorer shown to act this way. These observations will certainly facilitate the development of synthetic fertility restorers for CMS systems in which efficient natural Rfs are lacking.

plant biology↗

Rerouting of ribosomal proteins into splicing in plant organelles

Production and expression of RNAs requires the action of multiple RNA-binding proteins (RBPs). New RBPs are most often created by novel combinations of dedicated RNA binding modules. However, recruiting existing genes to create new RBPs is also an important evolutionary strategy. In this report, we analysed the 8-member uL18 ribosomal protein family in Arabidopsis. uL18 proteins share a short structurally conserved domain that binds the 5S rRNA and allow its incorporation into ribosomes. Our results indicate that Arabidopsis uL18-like proteins are targeted to either mitochondria or chloroplasts. While two members of the family are found in organelle ribosomes, we reveal that two uL18-type proteins correspond to splicing factors that are necessary for the elimination of certain mitochondrial and plastid group II introns. These two proteins do not co-sediment with mitochondrial or plastid ribosomes but associate with the introns whose splicing they promote. Our study thus reveals that the RNA binding capacity of uL18 ribosomal proteins has been detoured to create factors facilitating the elimination of organellar introns.

molecular biology↗