Comparative Analyses of Hairpin Substrate Recognition by Escherichia coli and Bacillus subtilis Ribonuclease P Ribozymes
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Summary
The results of kinetic studies showed that the metal ion concentration affected both the catalysis and the affinity of the ribozymes toward a hairpin RNA substrate.
- Type
- article
- Published
- 2003-01-01
- Cited by
- 5
- References
- 24
- Access
- Open access
- OpenAlex
- https://openalex.org/W2043455749
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1231232
Keywords
Ribozyme, Bacillus subtilis, RNase P, Escherichia coli, Ribonuclease
References
- Compilation of tRNA sequences and sequences of tRNA genes
- Guide DNA technique reveals that the protein component of bacterial ribonuclease P is a modifier for substrate recognition
- Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme
- 11 Structure and Mechanism of the Large Catalytic RNAs: Group I and Group II Introns and Ribonuclease P
- In vitro hyperprocessing of Drosophila tRNAs by the catalytic RNA of RNase P the cloverleaf structure of tRNA is not always stable?
- Recent studies of RNase P : tRNA Structure, Biosynthesis and Function
- Hyperprocessing of tRNA by the catalytic RNA of RNase P. Cleavage of a natural tRNA within the mature tRNA sequence and evidence for an altered conformation of the substrate tRNA.
- Ribonuclease P: function and variation.
- Mg2+-dependent folding of a large ribozyme without kinetic traps
- Nucleotide sequence and secondary structure of citrus exocortis and chrysanthemum stunt viroid.
- Kinetics of Hyperprocessing Reaction of Human Tyrosine tRNA by Ribonuclease P Ribozyme from Escherichia coli
- Another cut for lysine tRNA: application of the hyperprocessing reaction reveals another stabilization strategy in metazoan lysine tRNAs.
- Human Tyrosine tRNA Is Also Internally Cleavable by E. coli Ribonuclease P RNA Ribozyme in Vitro
- Hyperprocessing reaction of tRNA by Bacillus subtilis ribonuclease P ribozyme
- RNase P RNAs from some Archaea are catalytically active.
- Substrate shape specificity of E coli RNase P ribozyme is dependent on the concentration of magnesium ion.
- The varieties of ribonuclease P.
- Escherichia coli tRNAs Are Resistant to the Hyperprocessing Reaction of Homologous E. coli Ribonuclease P Ribozyme
- Guide DNA technique in bacterial ribonuclease P reaction for effective processing of tRNA precursor
- Recent Studies of RNase P
Cited by
- The Natural Intron Sequence of Human Tyrosine Pre-transfer RNA Is Not a Temporal Stabilizer for Cloverleaf Structure
- The Protein Component of Bacterial Ribonuclease P Flickers the Metal Ion Response to the Substrate Shape Preference of the Ribozyme
- Examining the Bases of the J3⁄4 Domain of Escherichia coli Ribonuclease P
- Substrate Shape Preference of Escherichia coli Ribonuclease P Ribozyme and Holo Enzyme Using Bottom-Half Part-Shifting Variants of Pre-tRNA
- The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced
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