@article {404,
	title = {A tyrosyl-tRNA synthetase recognizes a conserved tRNA-like structural motif in the group I intron catalytic core.},
	journal = {Cell},
	volume = {87},
	number = {6},
	year = {1996},
	month = {1996 Dec 13},
	pages = {1135-45},
	abstract = {The Neurospora crassa mitochondrial (mt) tyrosyl-tRNA synthetase (CYT-18 protein) functions in splicing group I introns, in addition to aminoacylating tRNA(Tyr). Here, we compared the CYT-18 binding sites in the N. crassa mt LSU and ND1 introns with that in N. crassa mt tRNA(Tyr) by constructing three-dimensional models based on chemical modification and RNA footprinting data. Remarkably, superimposition of the CYT-18 binding sites in the model structures revealed an extended three-dimensional overlap between the tRNA and the group I intron catalytic core. Our results provide insight into how an RNA-splicing factor can evolve from a cellular RNA-binding protein. Further, the structural similarities between group I introns and tRNAs are consistent with an evolutionary relationship and suggest a general mechanism for the evolution of complex catalytic RNAs.},
	keywords = {Base Sequence, Binding Sites, Biological Evolution, Conserved Sequence, Introns, Molecular Sequence Data, Neurospora crassa, Nucleic Acid Conformation, Protein Conformation, Protein Structure, Tertiary, RNA Splicing, RNA, Fungal, RNA, Transfer, Tyr, Tyrosine-tRNA Ligase},
	issn = {0092-8674},
	author = {Caprara, M G and Lehnert, V and Lambowitz, A M and Westhof, E}
}
