Results 1 to 10 of about 61,070 (218)
A tyrosyl-tRNA synthetase binds specifically to the group I intron catalytic core. [PDF]
Genes & Development, 1992 The Neurospora CYT-18 protein, the mitochondrial tyrosyl-tRNA synthetase, functions in splicing group I introns in mitochondria. Here, we show that CYT-18 binds strongly to diverse group I introns that have minimal sequence homology and recognizes highly conserved structural features of the catalytic core of these introns.
Qiang Guo, Alan M. Lambowitz
semanticscholar +5 more sources
Activation of the catalytic core of a group I intron by a remote 3' splice junction. [PDF]
Genes & Development, 1992 Over 1000 nucleotides may separate the ribozyme core of some group I introns from their 3' splice junctions. Using the sunY intron of bacteriophage T4 as a model system, we have investigated the mechanisms by which proximal splicing events are suppressed in vitro, as well as in vivo.
François Michel +6 more
semanticscholar +5 more sources
Evaluating Group I Intron Catalytic Efficiency in Mammalian Cells [PDF]
Molecular and Cellular Biology, 1999 Recent reports have demonstrated that the group I ribozyme from Tetrahymena thermophila can perform trans-splicing reactions to repair mutant RNAs. For therapeutic use, such ribozymes must function efficiently when transcribed from genes delivered to human cells, yet it is unclear how group I splicing reactions are influenced by intracellular ...
Meredith B. Long, Bruce A. Sullenger
semanticscholar +5 more sources
Pentamidine inhibits catalytic activity of group I intron Ca.LSU by altering RNA folding [PDF]
Nucleic Acids Research, 2002 The antimicrobial agent pentamidine inhibits the self-splicing of the group I intron Ca.LSU from the transcripts of the 26S rRNA gene of Candida albicans, but the mechanism of pentamidine inhibition is not clear. We show that preincubation of the ribozyme with pentamidine enhances the inhibitory effect of the drug and alters the folding of the ribozyme
Yi Zhang
semanticscholar +5 more sources
Catalytic activity is retained in theTetrahymenagroup I intron despite removal of the large extension of element P5 [PDF]
Nucleic Acids Research, 1989 We have made sizeable internal deletions within the self-splicing group I intron of Tetrahymena thermophila. Deletions were made in a piecewise manner in order to remove secondary structural elements thought to be extraneous to the catalytic center of the molecule.
Gerald F. Joyce, Gerda Horst, Tan Inoue
semanticscholar +6 more sources
Mechanism of 3' splice site selection by the catalytic core of the sunY intron of bacteriophage T4: the role of a novel base-pairing interaction in group I introns. [PDF]
Genes & Development, 1990 The catalytic core of the sunY intron of bacteriophage T4 is separated from its 3' exon by 837 nucleotides, most of which are part of an open reading frame (ORF). Here, we report that transcripts truncated within the sunY ORF self-splice in vitro to a variety of sites in the segment immediately 3' of the core. Recognition of these proximal splice sites
François Michel +3 more
semanticscholar +4 more sources
One RNA plays three roles to provide catalytic activity to a group I intron lacking an endogenous internal guide sequence [PDF]
Nucleic Acids Research, 2009 Catalytic RNA molecules possess simultaneously a genotype and a phenotype. However, a single RNA genotype has the potential to adopt two or perhaps more distinct phenotypes as a result of differential folding and/or catalytic activity. Such multifunctionality would be particularly significant if the phenotypes were functionally inter-related in a ...
Nilesh Vaidya, Niles Lehman
semanticscholar +5 more sources
Binding of the CBP2 protein to a yeast mitochondrial group I intron requires the catalytic core of the RNA. [PDF]
Genes & Development, 1991 The yeast CBP2 gene product is required for the splicing of the terminal intron (bI5) of the mitochondrial cytochrome b pre-mRNA in vivo. In vitro, bI5 RNA self-splices efficiently only at high MgCl2 concentrations (50 mM); at 5 mM MgCl2, efficient splicing requires purified CBP2 protein. To determine the sequences within bI5 recognized by the protein,
Alexandra Gampel, Thomas R. Cech
semanticscholar +4 more sources
A Tyrosyl-tRNA Synthetase Recognizes a Conserved tRNA-like Structural Motif in the Group I Intron Catalytic Core [PDF]
Cell, 1996 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.
Mark G. Caprara +3 more
semanticscholar +5 more sources
Cell, 1995 The yeast mitochondrial group I intron b15 undergoes self-splicing at high Mg2+ concentrations, but requires the splicing factor CBP2 for reaction under physiological conditions. Chemical accessibility and UV cross-linking experiments now reveal that self-processing is slow because functional elements are not properly positioned in an active tertiary ...
Kevin M. Weeks, Thomas R. Cech
semanticscholar +5 more sources