@article {379,
	title = {tRNA-like recognition of group I introns by a tyrosyl-tRNA synthetase.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {99},
	number = {5},
	year = {2002},
	month = {2002 Mar 5},
	pages = {2630-5},
	abstract = {The Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) functions in splicing group I introns by promoting the formation of the catalytically active RNA structure. Previous work suggested that CYT-18 recognizes a conserved tRNA-like structure of the group I intron catalytic core. Here, directed hydroxyl-radical cleavage assays show that the nucleotide-binding fold and C-terminal domains of CYT-18 interact with the expected group I intron cognates of the aminoacyl-acceptor stem and D-anticodon arms, respectively. Further, three-dimensional graphic modeling, supported by biochemical data, shows that conserved regions of group I introns can be superimposed over interacting regions of the tRNA in a Thermus thermophilus TyrRS/tRNA(Tyr) cocrystal structure. Our results support the hypothesis that CYT-18 and other aminoacyl-tRNA synthetases interact with group I introns by recognizing conserved tRNA-like structural features of the intron RNAs.},
	keywords = {Cloning, Molecular, Cysteine, Hydroxyl Radical, Introns, Models, Molecular, Neurospora crassa, Nucleic Acid Conformation, Protein Structure, Quaternary, RNA, Transfer, Tyrosine-tRNA Ligase},
	issn = {0027-8424},
	doi = {10.1073/pnas.052596299},
	author = {Myers, Christopher A and Kuhla, Birte and Cusack, Stephen and Lambowitz, Alan M}
}
