@article {425,
	title = {The neurospora CYT-18 protein suppresses defects in the phage T4 td intron by stabilizing the catalytically active structure of the intron core.},
	journal = {Cell},
	volume = {69},
	number = {3},
	year = {1992},
	month = {1992 May 1},
	pages = {483-94},
	abstract = {The Neurospora CYT-18 protein, a tyrosyl-tRNA synthetase, which functions in splicing group I introns in mitochondria, promotes splicing of mutants of the distantly related bacteriophage T4 td intron. In an in vivo assay, wild-type CYT-18 protein expressed in E. coli suppressed mutations in the td intron{\textquoteright}s catalytic core. CYT-18-suppressible mutations were also suppressed by high Mg2+ or spermidine in vitro, suggesting they affect intron structure. Both the N- and C-terminal domains of CYT-18 are required for efficient splicing, but CYT-18 with a large C-terminal truncation retains some activity. Our results indicate that CYT-18 interacts with conserved structural features of group I introns, and they provide direct evidence that a protein promotes splicing by stabilizing the catalytically active structure of the intron RNA.},
	keywords = {Base Sequence, Fungal Proteins, Genes, Suppressor, Genes, Viral, Introns, Molecular Sequence Data, Molecular Structure, Neurospora crassa, RNA Splicing, RNA, Viral, Spermidine, T-Phages, Tyrosine-tRNA Ligase, Viral Structural Proteins},
	issn = {0092-8674},
	author = {Mohr, G and Zhang, A and Gianelos, J A and Belfort, M and Lambowitz, A M}
}
