Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.26.5 (
RNase P
)
1,348
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
RNase P
and ribosomes must interact with similar substrate molecules, tRNA precursors in the case of
RNase P
and aminoacyl-, peptidyl- or free tRNAs in the case of ribosomes. In order to compare the substrate recognition mechanisms between ribosomes and
RNase P
, protein synthesis inhibitors have been assayed for their effect on the catalytic activity of the RNA component of Escherichia coli
RNase P
(M1 RNA).
Puromycin
has an inhibitory effect that could be related to similar substrate recognition mechanisms by rRNA in the ribosome and by M1 RNA in
RNase P
.
...
PMID:Protein synthesis inhibitors and catalytic RNA. Effect of puromycin on tRNA precursor processing by the RNA component of Escherichia coli RNase P. 246 23
Ribonuclease P (
RNase P
) is responsible for the generation of mature 5' termini of tRNA. The RNA component of this complex encodes the enzymatic activity in bacteria and is itself catalytically active under appropriate conditions in vitro. The role of the subunits in eucaryotes has not yet been established. We have partially purified
RNase P
activity from the ciliate protozoan Tetrahymena thermophila to learn more about the biochemical characteristics of
RNase P
from a lower eucaryote. The Tetrahymena
RNase P
displays a pH optimum and temperature optimum characteristic of
RNase P
enzymes isolated from other organisms. The Km of the T. thermophila enzyme for pre-tRNAGln is 1.6 x 10(-7)M, which is comparable to the values reported for other examples of
RNase P
. The Tetrahymena
RNase P
is a ribonucleoprotein complex, as supported by its sensitivity to micrococcal nuclease and proteinase K. The buoyant density of the enzyme in Cs2SO4 is 1.42 g/ml, which suggests that the RNA component of the Tetrahymena enzyme comprises a significantly greater percentage of the holoenzyme than that determined for
RNase P
of other Eucarya or Archaea. The holoenzyme has a requirement for divalent cations displaying characteristics that are unique for
RNase P
but closely resemble preferences reported for the Tetrahymena group I intron RNA.
Puromycin
inhibits pre-tRNA processing by the Tetrahymena complex, and implications of the similarities between recognition of tRNA by ribosomal components and
RNase P
are discussed.
...
PMID:Ribonuclease P of Tetrahymena thermophila. 866 80
