@article {415,
	title = {A tyrosyl-tRNA synthetase can function similarly to an RNA structure in the Tetrahymena ribozyme.},
	journal = {Nature},
	volume = {370},
	number = {6485},
	year = {1994},
	month = {1994 Jul 14},
	pages = {147-50},
	abstract = {Group I introns are highly structured RNAs which catalyse their own splicing by guanosine-initiated transesterification reactions. Their catalytic core is generally stabilized by RNA-RNA interactions within the core and with peripheral RNA structures. Additionally, some group I introns require proteins for efficient splicing in vivo. The Neurospora CYT-18 protein, the mitochondrial tyrosyl-transfer RNA synthetase (mt TyrRS), promotes splicing of the Neurospora mitochondrial large ribosomal RNA (LSU) and other group I introns by stabilizing the catalytically active structure of the intron core. We report here that CYT-18 functions similarly to a peripheral RNA structure, P5abc, that stabilizes the catalytic core of the Tetrahymena LSU intron. The CYT-18 protein and P5abc RNA bind to overlapping sites in the intron core, inducing similar conformational changes correlated with splicing activity. Our results show that a protein can play the role of an RNA structure in a catalytic RNA, a substitution postulated for the evolution of nuclear pre-messenger RNA introns from self-splicing introns.},
	keywords = {Animals, Base Sequence, Fungal Proteins, Introns, Molecular Sequence Data, Neurospora, Nucleic Acid Conformation, Protein Binding, RNA, Catalytic, RNA, Protozoan, Tetrahymena, Tyrosine-tRNA Ligase},
	issn = {0028-0836},
	doi = {10.1038/370147a0},
	author = {Mohr, G and Caprara, M G and Guo, Q and Lambowitz, A M}
}
