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 ...
M B, Long, B A, Sullenger
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Functional Identification of Ligands for a Catalytic Metal Ion in Group I Introns [PDF]
Biochemistry, 2008 Many enzymes use metal ions within their active sites to achieve enormous rate acceleration. Understanding how metal ions mediate catalysis requires elucidation of metal ion interactions with both the enzyme and the substrate(s). The three-dimensional arrangement determined by X-ray crystallography provides a powerful starting point for identifying ...
Marcello, Forconi +4 more
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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 +3 more
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Folding of group I introns from bacteriophage T4 involves internalization of the catalytic core. [PDF]
Proceedings of the National Academy of Sciences, 1991 Fe(II)-EDTA, a solvent-based cleavage reagent that distinguishes between the inside and outside surfaces of a folded RNA molecule, has revealed some of the higher-order folding of the group IB intron from Tetrahymena thermophila pre-rRNA. This reagent has now been used to analyze the bacteriophage T4 sunY and td introns, both of which are members of ...
T S, Heuer +4 more
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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.
Q, Guo, A M, Lambowitz
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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.
G F, Joyce, G, van der Horst, T, Inoue
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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.
Caprara, Mark G +3 more
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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.
F, Michel +6 more
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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 ...
Vaidya, Nilesh, Lehman, Niles
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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,
A, Gampel, T R, Cech
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