@article {436,
	title = {Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases.},
	journal = {Cell},
	volume = {62},
	number = {4},
	year = {1990},
	month = {1990 Aug 24},
	pages = {745-55},
	abstract = {Neurospora mitochondrial tyrosyl-tRNA synthetase (mt TyrRS), which is encoded by nuclear gene cyt-18, functions in splicing group I introns. Analysis of intragenic partial revertants of the cyt-18-2 mutant and in vitro mutants of the cyt-18 protein expressed in E. coli showed that splicing activity of the cyt-18 protein is dependent on a small N-terminal domain that has no homolog in bacterial or yeast mt TyrRSs. This N-terminal splicing domain apparently acts together with other regions of the protein to promote splicing. Our findings support the hypothesis that idiosyncratic sequences in aminoacyl-tRNA synthetase may function in processes other than aminoacylation. Furthermore, they suggest that splicing activity of the Neurospora mt TyrRs was acquired after the divergence of Neurospora and yeast, and they demonstrate one mechanism whereby splicing factors may evolve from cellular RNA binding proteins.},
	keywords = {Amino Acid Sequence, Amino Acyl-tRNA Synthetases, Base Sequence, Genes, Fungal, Mitochondria, Molecular Sequence Data, Molecular Weight, Mutation, Neurospora, Neurospora crassa, Phenotype, Protein Conformation, RNA Splicing, Spectrum Analysis, Structure-Activity Relationship, Tyrosine, Tyrosine-tRNA Ligase},
	issn = {0092-8674},
	author = {Cherniack, A D and Garriga, G and Kittle, J D and Akins, R A and Lambowitz, A M}
}
