Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.5 (RNase P)
 1,348 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

E. coli strain A49 carries the themosensitive mutation in the rnpA gene encoding the protein component of RNase P, a tRNA-processing enzyme. Two small RNAs were highly accumulated in the A49 carrying derivatives of ColE1-type plasmids, at nonpermissive temperature. Characterization of these RNAs showed that they were the processed or degraded products derived from RNA I, which is the negative controller of ColE1-type plasmid replication. These derivatives of RNA I only differ in size at the 5' ends. The data of their degradation and synthesis kinetics suggest that they are intermediates of RNA I metabolism.
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PMID:Alteration of RNA I metabolism in a temperature-sensitive Escherichia coli rnpA mutant strain. 138 Aug 3

Deletion derivatives of C5 protein, the protein cofactor of Escherichia coli RNase P, were constructed as soluble MBP (maltose-binding protein) fusion proteins to assess the deletion effects on promoting RNase P catalysis and on binding to M1 RNA, the catalytic subunit of the enzyme. The C5 protein, with large terminal deletions, retained its promoting activity of RNase P catalysis under protein excess conditions in vitro. Some deletion derivatives complemented the temperature sensitive phenotype of E. coli A49 cells carrying the rnpA49 mutation. This ability also suggests that part of the C5 protein is enough to produce the catalytic activity of RNase P in vivo. Both the central conserved region, called the RNR motif, and the C-terminal region are essential for the binding of C5 protein to M1 RNA. Meanwhile, the N-terminal region contributes to promoting RNase P catalysis in ways other than binding to M1 RNA.
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PMID:Effects of terminal deletions in C5 protein on promoting RNase P catalysis. 1065 23

Ribonuclease P (RNase P) is a ribonucleoprotein that requires magnesium ions to catalyze the 5' maturation of transfer RNA. To identify interactions essential for catalysis, the properties of RNase P containing single sulfur substitutions for nonbridging phosphodiester oxygens in helix P4 of Bacillus subtilis RNase P were analyzed using transient kinetic experiments. Sulfur substitution at the nonbridging oxygens of the phosphodiester bond of nucleotide U51 only modestly affects catalysis. However, phosphorothioate substitutions at A49 and G50 decrease the cleavage rate constant enormously (300-4,000-fold for P RNA and 500-15,000-fold for RNase P holoenzyme) in magnesium without affecting the affinity of pre-tRNA(Asp), highlighting the importance of this region for catalysis. Furthermore, addition of manganese enhances pre-tRNA cleavage catalyzed by B. subtilis RNase P RNA containing an Sp phosphorothioate modification at A49, as observed for Escherichia coli P RNA [Christian et al., RNA, 2000, 6:511-519], suggesting that an essential metal ion may be coordinated at this site. In contrast, no manganese rescue is observed for the A49 Sp phosphorothioate modification in RNase P holoenzyme. These differential manganese rescue effects, along with affinity cleavage, suggest that the protein component may interact with a metal ion bound near A49 in helix P4 of P RNA.
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PMID:Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P. 1216 48

The rnpA mutation, A49, in Escherichia coli reduces the level of RNase P at 43 degrees C because of a temperature-sensitive mutation in C5 protein, the protein subunit of the enzyme. Microarray analysis reveals the expression of several noncoding intergenic regions that are increased at 43 degrees C compared with 30 degrees C. These regions are substrates for RNase P, and they are cleaved less efficiently than, for example, tRNA precursors. An analysis of the tna, secG, rbs, and his operons, all of which contain RNase P cleavage sites, indicates that RNase P affects gene expression for regions downstream of its cleavage sites.
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PMID:A specific endoribonuclease, RNase P, affects gene expression of polycistronic operon mRNAs. 1458 31