RT Journal Article
SR Electronic
T1 Rerouting of ribosomal proteins into splicing in plant organelles
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.03.03.974766
DO 10.1101/2020.03.03.974766
A1 Chuande Wang
A1 Rachel Fourdin
A1 Martine Quadrado
A1 Céline Dargel-Graffin
A1 Dimitri Tolleter
A1 David Macherel
A1 Hakim Mireau
YR 2020
UL http://biorxiv.org/content/early/2020/03/05/2020.03.03.974766.abstract
AB 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.