rnpA Antibody

1. The comparative biology of Escherichia coli RNase P and Arabidopsis thaliana PRORP isozymes has been reported. PMID: 28499021
2. The ability of RNase P to initiate tRNA processing at the 3' ends of long primary transcripts by endonucleolytically removing the Rho-independent transcription terminator represents a previously unidentified function for the enzyme. PMID: 25183518
3. Rules govern substrate recognition by C5, which reveal specificity that is hidden in cellular substrates for RNase P; nonspecific and specific RNA-binding modes may not differ fundamentally, but represent distinct parts of common affinity distributions. PMID: 24056935
4. C5 protein has evolved to compensate for tRNA variation at positions important for binding to P RNA, allowing for tRNA specialization PMID: 19917291
5. results showed the presence of a bulge at U69 in the P4 domain was important in the holo enzyme; the conserved bases G63 and G64 in the J3/4 domain were important for efficient ribozyme reactions; domains displayed different responses to metal ions PMID: 15215612
6. 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 PMID: 15527768
7. data indicate that the conserved AGGA sequence was important for efficient ribozyme reactions, and suggested that the length mutations affected ribozyme activity through metal ion binding steps PMID: 15618639
8. RNase P from Escherichia coli cleaves the coenzyme B12 riboswitch from E. coli and a similar one from Bacillus subtilis. PMID: 16061811
9. RNase P stabilizes the global structure of RNase P RNA, and influences holoenzyme dimer formation and precursor tRNA. PMID: 16163391
10. RNAs in a T-shape structure can be substrates for the ribozyme reactions even at low concentrations of magnesium ions, and the RNA in a natural L-shape is the best substrate for both the ribozyme and the holo enzyme. PMID: 16244456
11. assembly of the E. coli RNase P holoenzyme involves RNA-dependent folding and stabilization of C5 protein PMID: 16750220
12. analysis of antisense inhibition of RNase P PMID: 16901906
13. Cognate protein subunit C5 enhances metal ion affinity in the active site of RNAase P, and thus is likely to contribute significantly to rate enhancement at physiological metal ion concentrations. PMID: 17652407
14. Description for the first time of a previously unidentified pathway for the maturation of tRNAs in polycistronic operons where the processing of the primary transcripts only involves RNase P. PMID: 17981836
15. These results demonstrate that the C5 protein metabolically stabilizes M1 RNA in the cell. PMID: 19114042

Show More

Hide All

KEGG: ecj:JW3681

STRING: 316385.ECDH10B_3890