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The  Neurospora crassa  mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) promotes the splicing of group I introns by stabilizing the catalytically active RNA structure. To accomplish this, CYT-18 recognizes conserved structural features of group I intron RNAs using regions of the N-terminal nucleotide-binding fold, intermediate α-helical, and C-terminal RNA-binding domains that also function in binding tRNA Tyr . Curiously, whereas the splicing of the  N. crassa  mitochondrial large subunit rRNA intron is completely dependent on CYT-18’s C-terminal RNA-binding domain, all other group I introns tested thus far are spliced efficiently by a truncated protein lacking this domain. To investigate the function of the C-terminal domain, we used an  Escherichia coli  genetic assay to isolate mutants of the  Saccharomyces cerevisiae  mitochondrial large subunit rRNA and phage T4  td  introns that can be spliced in vivo by the wild-type CYT-18 protein, but not by the C-terminally truncated protein. Mutations that result in dependence on CYT-18’s C-terminal domain include those disrupting two long-range GNRA tetraloop/receptor interactions: L2–P8, which helps position the P1 helix containing the 5′-splice site, and L9–P5, which helps establish the correct relative orientation of the P4–P6 and P3–P9 domains of the group I intron catalytic core. Our results indicate that different structural mutations in group I intron RNAs can result in dependence on different regions of CYT-18 for RNA splicing.

The Neurospora crassa CYT-18 protein C-terminal RNA-binding domain helps stabilize interdomain tertiary interactions in group I introns