@article{,
title = {A tyrosyl-tRNA synthetase recognizes a conserved tRNA-like structural motif in the group I intron catalytic core},
author = {M G Caprara and V Lehnert and A M Lambowitz and E Westhof},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8978617},
isbn = {8978617},
year = {1996},
date = {1996-01-01},
journal = {Cell},
volume = {87},
number = {6},
pages = {1135-1145},
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.},
note = {0092-8674
Journal Article},
keywords = {Base Sequence Binding Sites/genetics Conserved Sequence Evolution *Introns Molecular Sequence Data Neurospora crassa Nucleic Acid Conformation Protein Conformation Protein Structure, Fungal/chemistry/metabolism/physiology RNA, Non-U.S. Gov't Support, P.H.S. Tyrosine-tRNA Ligase/*chemistry/*genetics/metabolism, Tertiary RNA Splicing/physiology RNA, Transfer, Tyr/chemistry Support, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
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.