The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced
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Summary
The results indicated that mutations in the P3 domain did not affect the cleavage site selection of the pre‐tRNA substrate, but did affect the efficiency of cleavage of the substrate.
- Type
- article
- Published
- 2004-11-05
- Cited by
- 3
- References
- 19
- Access
- Open access
- OpenAlex
- https://openalex.org/W2086770080
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:45998626
Keywords
Ribonuclease, Chemistry, Domain (mathematical analysis), Ribonuclease III, RNA
References
- Guide DNA technique reveals that the protein component of bacterial ribonuclease P is a modifier for substrate recognition
- Base pairing between Escherichia coli RNase P RNA and its substrate.
- Trna: Structure, Biosynthesis, and Function
- Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme
- 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
- 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.
- Comparative Analyses of Hairpin Substrate Recognition by Escherichia coli and Bacillus subtilis Ribonuclease P Ribozymes
- Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA.
- Three-dimensional working model of M1 RNA, the catalytic RNA subunit of ribonuclease P from Escherichia coli.
- Specific binding of arginine to TAR RNA.
- The P15-loop of Escherichia coli RNase P RNA is an autonomous divalent metal ion binding domain.
- Protein Components Contribute to Active Site Architecture for Eukaryotic Ribonuclease P*
- Bacterial ribonuclease P holoenzyme crosslinking analysis reveals protein interaction sites on the RNA subunit.
- Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme.
- Phylogenetic-comparative analysis of the eukaryal ribonuclease P RNA.
- Recent Studies of RNase P
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