Results 181 to 190 of about 60,524 (204)
Genome-wide identification and unveiling the role of MAP kinase cascade genes involved in sugarcane response to abiotic stressors. [PDF]
Ali A+9 more
europepmc +1 more source
Minimal catalytic domain of a group I self-splicing intron RNA. [PDF]
The self-splicing intron ribozymes have been regarded as primitive forms of the splicing machinery for eukaryotic pre-mRNAs. The splicing activity of group I self-splicing introns is dependent on an absolutely conserved and exceptionally densely packed core region composed of two helical domains, P3-P7 and P4-P6, that are connected rigidly via base ...
Tan Inoue+2 more
semanticscholar +4 more sources
Footprinting the Sites of Interaction of Antibiotics with Catalytic Group I Intron RNA [PDF]
Aminoglycoside inhibitors of translation have been shown previously to inhibit in vitro self-splicing by group I introns. Chemical probing of the phage T4-derived sunY intron shows that neomycin, streptomycin, and related antibiotics protected the N-7 position of G96, a universally conserved guanine in the binding site for the guanosine ...
Uwe von Ahsen, H F Noller
semanticscholar +4 more sources
A 3′ splice site-binding sequence in the catalytic core of a group I intron
Ribozymes use specific RNA-RNA interactions for substrate binding and active-site formation. Self-splicing group I introns have approximately 70 nucleotides constituting the core, a region containing sequences and structures indispensable for catalytic function.
John M. Burke+3 more
semanticscholar +5 more sources
A minor groove RNA triple helix within the catalytic core of a group I intron [PDF]
Close packing of several double helical and single stranded RNA elements is required for the Tetrahymena group I ribozyme to achieve catalysis. The chemical basis of these packing interactions is largely unknown. Using nucleotide analog interference suppression (NAIS), we demonstrate that the P1 substrate helix and J8/7 single stranded segment form an ...
Alexander A. Szewczak+4 more
semanticscholar +4 more sources
A Tyrosyl-tRNA Synthetase Protein Induces Tertiary Folding of the Group I Intron Catalytic Core
The Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) functions in splicing group I introns. We have used chemical-structure mapping and footprinting to investigate the interaction of the CYT-18 protein with the N. crassa mitochondrial large subunit ribosomal RNA (mt LSU) and ND1 introns, which are not detectably self-splicing in
Mark G. Caprara+2 more
semanticscholar +5 more sources
Minimum secondary structure requirements for catalytic activity of a self-splicing group I intron
We have completed a comprehensive deletion analysis of the Tetrahymena ribozyme in order to define the minimum secondary structure requirements for phosphoester transfer activity of a self-splicing group I intron. A total of 299 nucleotides were removed in a piecewise fashion, leaving a catalytic core of 114 nucleotides that form 7 base-paired ...
Amber Beaudry, Gerald F. Joyce
semanticscholar +5 more sources
The Neurospora crassa mitochondrial tyrosyl-tRNA synthetase, the CYT-18 protein, functions in splicing group I introns by promoting the formation of the catalytically active structure of the intron RNA. The group I intron catalytic core is thought to consist of two extended helical domains, one formed by coaxial stacking of P5, P4, P6, and P6a (P4-P6 ...
Christopher A. Myers+6 more
semanticscholar +5 more sources
The recent increase in the population of immunocompromised patients has led to an insurgence of opportunistic human fungal infections. The lack of effective treatments against some of these pathogens makes it important to develop new therapeutic strategies. One such strategy is to target key RNAs with antisense compounds. We report the development of a
Stephen M. Testa+3 more
semanticscholar +5 more sources
Two adenosine residues, universally conserved among group I introns, are located in the L4 region of the catalytic core. Base-substitution mutations in these adenosines resulted in diminished in vitro self-splicing activity of the Tetrahymena group I intron, more severely for double than for single mutations. The defect caused by the mutation of the L4
Kelly P. Williams+2 more
semanticscholar +5 more sources