Purine N7 groups that are crucial to the interaction of Escherichia coli RNase P RNA with tRNA

RNA

Volumn 7, Issue 7, 2001, Pages 958-968

  Heide, Corinna ^a   Feltens, Ralph ^a   Hartmann, Roland K ^a  

^a UNIVERSITY OF LÜBECK   (Germany)

Author keywords

c7 deaza interference; Gel retardation; Nucleotide analog interference mapping (NAIM); RNase P RNA

Indexed keywords

AMMONIA; CALCIUM; FUNCTIONAL GROUP; MAGNESIUM; NUCLEOTIDE; PURINE; RIBONUCLEASE P; RIBOZYME; SODIUM; SODIUM CHLORIDE; TRANSFER RNA;

ARTICLE; ASSAY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; NUCLEIC ACID ANALYSIS; PRIORITY JOURNAL; RNA BINDING; RNA PROCESSING;

BASE SEQUENCE; ENDORIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; PURINES; RIBONUCLEASE P; RNA, BACTERIAL; RNA, CATALYTIC; RNA, TRANSFER;

ESCHERICHIA COLI; PROKARYOTA;

EID: 0034962166     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838201001753     Document Type: Article

References (42)

1. The recognition by RNase P of precursor tRNAs
2. Defining functional groups, core structural features and inter-domain tertiary contacts essential for group II intron self-splicing: A NAIM analysis
3. The ribonuclease P database
4. Comparative analysis of ribonuclease RNase P RNA using gene sequences from natural microbial populations reveals tertiary structural elements
5. Mapping the active site of ribonuclease P RNA using a substrate containing a photoaffinity agent
6. 74 in the reaction catalyzed by Escherichia coli RNase P RNA
7. Comparative photocross-linking analysis of the tertiary structure of Escherichia coli and Bacillus subtilis RNase P RNAs
8. Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme
9. Identification of individual nucleotides in the bacterial ribonuclease P ribozyme adjacent to the pre-tRNA cleavage site by short-range photocross-linking
10. Contributions of phylogenetically variable structural elements to the function of the ribozyme ribonuclease P
11. Ribonuclease RNase P RNA: Models of the 15/16 bulge from Escherichia coli and the P15 stem loop of Bacillus subtilis
12. Ribonuclease P: Unity and diversity in a tRNA processing ribozyme
13. A physical assay for and kinetic analysis of the interactions between M1 RNA and tRNA precursor substrates
14. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
15. Evolutionary variation in bacterial RNase P RNAs
16. Further perspective on the catalytic core and secondary structure of ribonuclease RNase P RNA
17. Rp-deoxy-phosphorothioate modification interference experiments identify 2′-OH groups in RNase P RNA that are crucial to tRNA binding
18. Mutational analysis of the joining regions flanking helix P18 in E. coli RNase P RNA
19. Kinetics and thermodynamics of the RNase P RNA cleavage reaction: Analysis of tRNA 3′-end variants
20. Rp-phosphorothioate modifications in RNase P RNA that interfere with tRNA binding
21. Analysis of the tertiary structure of the ribonuclease P ribozyme-substrate complex by site-specific photoaffinity crosslinking
22. Use of photoaffinity crosslinking and molecular modeling to analyze the global architecture of ribonuclease P RNA
23. Identification of phosphates involved in catalysis by the ribozyme RNase P RNA
24. Distinct modes of mature and precursor tRNA binding to E. coli RNase P RNA revealed by NAIM analyses
25. 2 groups of Escherichia coli RNase P RNA involved in intramolecular tertiary contacts and direct interactions with tRNA
26. Identification by modification-interference of purine N-7 and ribose 2′-OH groups critical for catalysis by bacterial ribonuclease P
27. Base pairing between Escherichia coli RNase P RNA and its substrate
28. Different cleavage sites are aligned differently in the active site of M1 RNA, the catalytic subunit of Escherichia coli RNase P
29. Phylogenetic comparative chemical footprint analysis of the interaction between ribonuclease RNase P RNA and tRNA
30. Domain structure of the ribozyme from eubacterial ribonuclease P
31. Derivation of the three-dimensional architecture of bacterial ribonuclease RNase P RNAs from comparative sequence analysis
32. Characterization of the Borrelia burgdorferi RNase P RNA gene reveals a novel tertiary interaction
33. 2+ ions by ribonuclease P
34. Interaction of the 3′-end of tRNA with ribonuclease P RNA
35. Probing of tertiary interactions in RNA: 2′-hydroxyl-base contacts between the RNase P RNA and pre-tRNA
36. RNase P RNAs from some Archaea are catalytically active
37. Multiple binding modes of substrate to the catalytic RNA subunit of RNase P from Escherichia coli
38. Identification of adenosine functional groups involved in substrate binding by the ribonuclease P ribozyme
39. Multiple magnesium ions in the ribonuclease P reaction mechanism
40. Interaction between Escherichia coli RNase P RNA and the discriminator base results in slow product release
41. Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis
42. Mapping in three dimensions of regions in a catalytic RNA protected from attack by an Fe(II)-EDTA reagent