@article {456,
	title = {Protein-dependent splicing of a group I intron in ribonucleoprotein particles and soluble fractions.},
	journal = {Cell},
	volume = {46},
	number = {5},
	year = {1986},
	month = {1986 Aug 29},
	pages = {669-80},
	abstract = {The group I intron in the Neurospora mitochondrial large rRNA gene is not self-splicing in vitro. Here, we show that this intron can be spliced from 35S pre-rRNA in RNPs or from deproteinized 35S pre-rRNA or in vitro transcripts by a soluble activity that is present in mitochondrial lysates and can be released from RNPs. Splicing occurs by the same guanosine-initiated transesterification mechanism characteristic of self-splicing group I introns, but is absolutely dependent upon proteins that are presumably required for correct folding of the pre-rRNA. The soluble splicing activity is not simply associated with large subunit ribosomal proteins. Nuclear mutant cyt18-1, which is defective in splicing a number of group I introns in vivo, is grossly deficient in the soluble splicing activity. Our results suggest that the cyt18 gene encodes or regulates a component of an activity that functions in splicing group I introns in Neurospora mitochondria.},
	keywords = {Base Sequence, Fungal Proteins, Mitochondria, Neurospora, Neurospora crassa, Nucleic Acid Conformation, Nucleic Acid Precursors, Ribonucleoproteins, RNA, RNA Precursors, RNA Splicing, RNA, Fungal, RNA, Ribosomal},
	issn = {0092-8674},
	author = {Garriga, G and Lambowitz, A M}
}
