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metabolism
the enzyme is involved in maturation of the 5'-end of tRNA
evolution
comparison of nuclear, mitochondrial, and plastidic RPPs, overview
evolution
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Dictyostelium discoideum nuclear RNase P is a ribonucleoprotein complex that displays similarities with its counterparts from higher eukaryotes such as the human enzyme, but at the same time it retains distinctive characteristics
evolution
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evolutionary history of PRORP, overview
evolution
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identification in select archaea of an unusual archetype of the RNase P RNA
evolution
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the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
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the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
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the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
-
the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform different functions encompassing cell cycle control and stem cell biology. From archaeal RNase P to bacterial RNase P the protein complexitity in prokaryotic protein cofactors RNPs increases. Comparison to eukaryal RNase Ps. Diversification via RNAs
evolution
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in the evolved, modern RNase P enzymes, the RNA depends on protein to fulfill its cellular function. This RNA-based form of RNase P is found in all domains of life, but there is an apparent trend from RNA to protein predominance in the overall composition and functioning of these ribonucleoproteins from bacteria to eukarya. RNase P of the former is built from a catalytically proficient RNA and a single small protein only. RNase P RNA of Archaea is a less-efficient catalyst in vitro and associates with five proteins, none of which is related to the bacterial protein. Another entirely different form of RNase P, i.e. proteinaceous RNase P, apparently not containing RNA, is initially observed in the organelles of different eukarya, e.g. humans, and also in Trypanosoma brucei. The genomes of trypanosomatids lack evidence for genes related to RNA-based RNase P, but they encode two homologues of human and plant PRORP genes. Also in plants, all cellular tRNA 5' end maturation appears to be exclusively protein dependent
evolution
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the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
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the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
-
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview
evolution
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the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview. The chloroplast and mitochondrial genomes of Ostreococcus tauri encode distinct individual RNase P RNA genes and the nucleus encodes both a bacterial-like RNase P protein component, and a proteinaceous RNase P enzyme
evolution
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the enzyme is conserved in all domains of life. The composition of RNase P varies from bacteria to archaea and eukarya, evolutionary enzyme spread, overview. The protozoan Trypanosoma brucei harbors 2 PRORP isoforms, both of which have 5' pre-tRNA processing activity in vitro. One isoform (PRORP1) localizes to the nucleus and the second (PRORP2) to the mitochondrion
evolution
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two architectural subtypes of bacterial P RNAs, the phylogenetically prevailing ancestral type A represented by Escherichia coli P RNA, and Bacillus type B essentially confined to the low G + C Gram-positive bacteria, the prototype being Bacillus subtilis P RNA
evolution
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two architectural subtypes of bacterial P RNAs, the phylogenetically prevailing ancestral type A represented by Escherichia coli P RNA, and Bacillus type B essentially confined to the low G + C Gram-positive bacteria, the prototype being Bacillus subtilis P RNA
evolution
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Yeast RNase P has lost RNA elements that serve as structural braces in its bacterial and, by inference, archaeal counterparts, but has gained proteins Pop1, Pop6, Pop7 and Pop8 that are not found in archaea
evolution
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comparison of nuclear, mitochondrial, and plastidic RPPs, overview
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evolution
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Dictyostelium discoideum nuclear RNase P is a ribonucleoprotein complex that displays similarities with its counterparts from higher eukaryotes such as the human enzyme, but at the same time it retains distinctive characteristics
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malfunction
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genetic alterations in either the RNA or protein subunit impair enzyme activity in vitro. A structural mutation in the RNase P protein (temperature-sensitive mutant ts241) affects the RNase P RNA level in vivo
malfunction
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in a strain carrying the rnpA49 allele, encoding temperature sensitive RNase P, thermal inactivation of RNase P leads to ca. 60% reduction in relative quantities of the mature tRNA, although there is no change the relative quantities of the primary transcripts. Inactivation of both RNase P and RNase E leads to disappearance of the majority of the heterogeneous pre-tRNA precursor species except for the species containing the intact 5'-end and a processed 3'-end. In the absence of RNase P (both rnpA49 and rnpA49 rne-1) ca. 77% (36/49) of the transcripts have immature 3' termini containing 1-3 nt downstream of the CCA
malfunction
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in both deletion mutants Rpp20(16-140) and Rpp20(35-140) the global thermodynamics of the interaction with Rpp25 is seemingly unaffected. Thermodynamic signature of the association is also fully preserved between the Rpp25(25-170) mutant and all available versions of Rpp20. Regions within the mutants Rpp20(35-140) and Rpp25(25-170) are sufficient for mutual interaction, thus this recognition can be mediated largely, if not exclusively, by the Alba-type core domains
malfunction
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inactivation of RNase P results in decreased transcription of several non-coding RNAs in a cell cycle-dependent fashion
malfunction
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mutant M1-C2 is catalytically inactive
malfunction
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absence of the enzyme in mutant rnpA49 rph-1 strain results in accumulation of unprocessed large tRNA transcripts and a 4fold decrease in mature species
malfunction
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deletion of the S-domain reduces the activity rate, changes the Mg2+ requirement, and has a significant impact on the kinetic of cleavage for substrates carrying C-1/G+73. Substitutions in the truncated mutant, e.g. at pposition 248, can partly compensate for the absence of the S-domain, overview
malfunction
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mutations in the RNR motif of P protein alter the affinity of PRNA for P protein, and of RNase P for pre-tRNAAsp, overview
malfunction
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downregulation results in impaired tRNA biogenesis in both organelles and the nucleus
malfunction
in both plastids and mitochondria, the effects of PRORP1 knock-down on the processing of individual tRNA species are highly variable. While a few tRNAs are severely affected, many others show little or no changes in accumulation of the mature tRNA. The drastic reduction in the levels of mature plastid tRNA-Phe(GAA) and tRNA-Arg(ACG) suggests that these two tRNA species limit plastid gene expression in the PRORP1 mutants and, hence, are causally responsible for the mutant phenotype
malfunction
Chlamydomonas reinhardtii cw15 arg7-8 mt+
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downregulation results in impaired tRNA biogenesis in both organelles and the nucleus
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malfunction
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in a strain carrying the rnpA49 allele, encoding temperature sensitive RNase P, thermal inactivation of RNase P leads to ca. 60% reduction in relative quantities of the mature tRNA, although there is no change the relative quantities of the primary transcripts. Inactivation of both RNase P and RNase E leads to disappearance of the majority of the heterogeneous pre-tRNA precursor species except for the species containing the intact 5'-end and a processed 3'-end. In the absence of RNase P (both rnpA49 and rnpA49 rne-1) ca. 77% (36/49) of the transcripts have immature 3' termini containing 1-3 nt downstream of the CCA
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malfunction
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absence of the enzyme in mutant rnpA49 rph-1 strain results in accumulation of unprocessed large tRNA transcripts and a 4fold decrease in mature species
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physiological function
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an in vitro transcribed RNase P RNA is catalytically active
physiological function
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assembly of the mature RNase P RNA with its cognate protein subunit ensures longevity of the holoenzyme complex in vivo. Increased growth rate of the organism coincides with increased RNase P RNA copy number
physiological function
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binding of RPP29 to RPP21 involves binding-coupled folding and stabilization of interfacial structures in RPP29. When bound to its partner, RPP21 adopts the same overall L-shaped structure observed in the free protein: a long arm containing the two N-terminal alpha-helices, a short-arm made up of the C-terminal beta-sheet comprising the zinc ribbon, and a central linker connecting the two domains. In the complex, helix alpha1 of RPP21 extends through residues 9-17, indicating that binding is associated with induced fit in RPP21 as well. The N-terminal region of RPP29 extends in an antiparallel fashion along RPP21 helix alpha1. RPP29 beta2 interacts with both helices of RPP21 in the center of the interface, and the C-terminal helix of RPP29 stabilizes the end of RPP21 helix alpha2. The RPP21RPP29 complex is localized to the specificity domain of the RNase P RNA. Sm-like core of RPP29 is essentially unchanged by RPP21 binding
physiological function
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Ignicoccus hospitalis is the host of Nanoarchaeum equitans, who has no RNase P and is dependent on its host RNase P activity for transfer of metabolites, energy and amino acids
physiological function
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in the presence of the RPP29RPP21 complex, the paired regions P9, P10/11, and P12 in the S-domain are protected from V1 cleavage, while no protection by RPP29RPP21 complex is observed in the C-domain
physiological function
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mitochondrial RNase P RNA is primitive and recognizably similar to those of alpha-proteobacteria, the ancestors of mitochondria
physiological function
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native nuclear RNase P has an RNase P RNA plus nine RNase P proteins. All subunits are essential for RNase P activity and cell viability. Only the nuclear-encoded RPM2 is known and shown genetically to be required for mitochondrial RNase P activity
physiological function
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native nuclear RNase P has an RNase P RNA plus ten RNase P proteins. The protein-only mitochondrial RNase P is composed of three proteins (MRPP1-MRPP3). MRPP1, which methylates G9 of tRNAs, may be responsible for substrate recognition. RNase P RNA is weakly active without RNase P proteins, some activity is present when reconstituted with RPP21 and RPP29
physiological function
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plastid RNase P RNA in the non-green alga is similar to those of their cyanobacterial ancestry
physiological function
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RNase P is an essential enzyme that catalyzes the 5' endonucleolytic cleavage of pre-tRNAs. RNase MRP, a variant of RNase P that has evolved to participate in ribosomal RNA processing, is also involved in turnover of specific messenger RNAs. RNase P and RNase MRP have eight proteins in common, with the RNA subunits being related but diverged. RNase P has one distinctive protein subunit (Rpr2p), while RNase MRP has two (Snm1p, Rmp1p). Nuclear RNase P is involved in a pathway for alternative maturation of intron-encoded box C/D snoRNAs
physiological function
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RNase P is required in all free-living cells, RNase P is encoded even in the most compact bacterial genome of Mycoplasma genitalium
physiological function
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Salmonella can efficiently deliver RNase P-based ribozyme sequence in specific human cells, leading to substantial ribozyme expression and effective inhibition of viral infection: targeted gene delivery of RNase P ribozyme by Salmonella to human cytomegalovirus-infected cells results in effective inhibition of viral gene expression and replication. Functional RNase P ribozyme (M1GS RNA) that targets the overlapping mRNA region of two human cytomegalovirus capsid proteins, the capsid scaffolding protein and assemblin, which are essential for viral capsid formation. A reduction of 87-90% in viral capsid scaffolding protein expression and a reduction of about 5000fold in viral growth in cells that are treated with Salmonella carrying the sequence of the functional ribozyme
physiological function
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strong interaction between Rpp25 and Rpp20. Rpp20 and Rpp25 interact with the P3 arm of RNase MRP RNA in a highly synergic fashion. Rpp20 and Rpp25 interact with the P3 RNA as a heterodimer, which is formed prior to RNA binding. Association between Rpp20 and Rpp25 has no detectable influence on their secondary/tertiary structure. The association reaction results in a large loss of solvent-accessible area. N- and C-terminal regions of Rpp25 and the N-terminal tail of Rpp20 are not involved in mutual recognition
physiological function
-
the holoenzyme consists of a single RNase P RNA associated with RNase P protein subunits
physiological function
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the mitochondrial RNase P is devoid of any RNA, mitochondria make their RNase P of three proteins only. MRPP1 is involved in the methylation of G9 in mitochondria in addition to its role in mitochondrial RNase P. MRRP2 may contribute RNA binding activity to mitochondrial RNase P via its conserved NAD+-binding domain. In its C-terminal half MRPP3 displays a handful of amino acid residues strictly conserved in their identity and spacing and reminiscent of a metallonuclease's active site: three aspartates and a histidine, the latter proposed to be directly involved in catalysis
physiological function
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the nuclear holoenzyme is comprised of protein subunits and RNase P RNA. In mitochondria, the usual RNA-containing RNase P is replaced by an enzyme composed of three proteins that are unrelated to RNase P enzymes in other systems (Rube Goldberg triad of unrelated proteins), but nevertheless are together responsible for the cleavage of pre-tRNA precursors
physiological function
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the organism has distinct RNase P enzymes in the nucleus and mitochondria. The RNase P RNA from the mitochondrion is an example of a highly-derived (degenerate) mitochondrial RNase P RNA
physiological function
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the RNase P holoenzyme is composed of a single RNA (type A1 RNase P RNA) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
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the RNase P holoenzyme is composed of a single RNA (type A2 RNase P RNA, lacks P13 and P14) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
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the RNase P holoenzyme is composed of a single RNA (type A3 RNase P RNA, with an altered L15 internal loop, in which the substrate 3'-NCCA tail is recognized) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type A4 RNase P RNA, with an altered L15) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
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the RNase P holoenzyme is composed of a single RNA (type A5 RNase P RNA, lacks P18) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type B1 RNase P RNA) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type B2 RNase P RNA, lacks P10.1) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type B3 RNase P RNA, lacks P12) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA (type C RNase P RNA) and a single small protein subunit. Bacterial RNase P RNAs are comprised of two independently evolving domains, separated by P7. The RNA upstream and downstream of P7 contains all of the essential catalytic sequences and structures (C-domain). Changes in the RNA bound at each end by the two strands of P7 (the loop of P7) alter substrate specificity (S-domain). The RNA subunit is associated with a single, small conservative protein, encoded by the rnpA gene, which has an unusual left-handed betaalphabeta crossover connection and a large central cleft
physiological function
-
the RNase P holoenzyme is composed of a single RNA molecule (type A RNase P RNA) and several protein subunits
physiological function
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the RNase P holoenzyme is composed of a single RNA molecule (type M RNase P RNA, lacking P6, P8, P16 and P17) and several protein subunits
physiological function
-
the RNase P holoenzyme is composed of a single RNA molecule (type T RNase P RNA, lacking the S-domain) and several protein subunits
physiological function
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Bacillus subtilis RNase P, composed of a catalytically active RNA, PRNA, and a small protein, the P protein, subunit, catalyzes the 5' end maturation of precursor tRNAs. Inner-sphere coordination of divalent metal ions to PRNA is essential for catalytic activity, but not for the formation of the RNase P/pre-tRNA complex. Previous studies have demonstrated that this RNase P/pre-tRNA complex undergoes an essential conformational change before the cleavage step. The RNase P/pre-tRNA conformer is stabilized by a high affinity divalent cation capable of inner-sphere coordination, such as Ca2+ or Mg2+. A second, lower affinity Mg2+ activates cleavage catalyzed by RNase P. Conformational changes and structural analysis, overview
physiological function
-
nuclear RNase P is required for transcription and processing of tRNA
physiological function
RNase P catalyzes 5'-maturation of tRNAs. Recombinant Ostreococcus tauri RPP can functionally reconstitute with bacterial RNase P RNAs but not with Ostreococcus tauri organellar RPRs, despite the latter's presumed bacterial origin
physiological function
-
RNase P is a catalytic ribonucleoprotein primarily involved in tRNA biogenesis. Insights into the role of protein cofactors RPPs in substrate recognition and cleavage-site selection. Cleavage of various model hairpin loop substrates in the presence of archaeal RPPs
physiological function
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RNase P is a ubiquitous and essential endoribonuclease. It is a catalytic ribonucleoprotein complex that employs an RNA catalyst and Mg2+ ions to cleave precursor RNAs (pre-RNAs) and generate the 5' termini of mature RNAs such as tRNA, 4.5S RNA, tmRNA, and other cellular RNAs
physiological function
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RNase P is an essential endoribonuclease processing the 59 leader of pre-tRNAs. Compared to bacterial RNase P, which contains a single small protein subunit and a large catalytic RNA subunit, eukaryotic nuclear RNase P is more complex, containing nine proteins and an RNA subunit in Saccharomyces cerevisiae. Nuclear RNase P has been shown to possess unique RNA binding capabilities, molecular recognition of nuclear RNase P, overview. Multiple interactions are required for high affinity binding
physiological function
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RNase P is an essential endoribonuclease that catalyzes the cleavage of the 59 leader of pre-tRNAs. In addition, a growing number of non-tRNA substrates are identified in various organisms. RNase P varies in composition, as bacterial RNase P contains a catalytic RNA core and one protein subunit, while eukaryotic nuclear RNase P retains the catalytic RNA but has at least nine protein subunits. The additional eukaryotic protein subunits most likely provide additional functionality to RNase P, with one possibility being additional RNA recognition capabilities
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
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RNase P plays a role in precursor tRNA processing
physiological function
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RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
-
RNase P plays a role in precursor tRNA processing
physiological function
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RNase P processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme. The RNA component catalyzes tRNA maturation in vitro without proteins
physiological function
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RNase P processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme. The RNA component catalyzes tRNA maturation in vitro without proteins
physiological function
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RNase P processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme. The RNA component catalyzes tRNA maturation in vitro without proteins
physiological function
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the RNR motif of RNase P protein interacts with both catalytic RNA PRNA and pre-tRNA to stabilize an active conformer
physiological function
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the stem loops of the RNase P RNA are required as binding sites for the proteins, their interactions are predominantly involved in stabilizing the active conformation of the enzyme
physiological function
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the ubiquitous endonuclease RNase P is responsible for the 5' maturation of tRNA precursors. In Arabidopsis thaliana mitochondria and plastids, a single protein called proteinaceous RNase P, PRORP1, can perform the endonucleolytic maturation of tRNA precursors that defines RNase P activity. In addition, PRORP1 is able to cleave tRNA-like structures involved in the maturation of plant mitochondrial mRNAs
physiological function
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ribonuclease P is a ribonucleoprotein complex involved in the processing of the 5'-leader sequence of precursor tRNA (pre-tRNA). RNaseP proteins are predominantly involved in optimization of the pRNA conformation, though they are individually dispensable for RNase P activity in vitro
physiological function
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the enzyme is involved in the procvessing of the leader sequence of precursor tRNA
physiological function
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ribonuclease P catalyzes the metal-dependent 5' end maturation of precursor tRNAs
physiological function
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RNase P is the endonuclease that removes 5' extensions from tRNA precursors, an early and essential step in tRNA biogenesis. PRORP1 Is able to substitute for Saccharomyces cerevisiae strain BY4743 nuclear RNase P in vivo, the inherently different physical qualities of the two enzyme forms are not reflected in a basically different functionality
physiological function
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the enzyme catalyzes the 5' end maturation of precursor tRNAs
physiological function
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the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
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the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
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the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
-
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs
physiological function
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the enzyme catalyzes the maturation of the 5' end of precursor-tRNAs. Trypanosoma brucei proteinaceous enzyme PRORP1 can substitute for yeast nuclear RNase P in vivo. Proteinaceous PRORP1 catalyzes all of the other noncanonical, yet vital functions of nuclear yeast RNase P, which may include processing of non-canonical RNAs
physiological function
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the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs
physiological function
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the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs
physiological function
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the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs
physiological function
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the enzyme catalyzes tRNA 5' maturation
physiological function
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the enzyme is a ribonuleoprotein that catalyzes the processing of 5' leader sequences from tRNA precursors and other noncoding RNA in all living cells
physiological function
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the enzyme is an essential ribonucleoprotein enzyme that is responsible for catalyzing the maturation of the 5' end of transfer RNAs through site-specific hydrolysis of a phosphodiester bond in precursor tRNAs. The single enzyme processes the 5' ends of tRNA precursors in cells and organelles that carry out tRNA biosynthesis. Rates of ptRNA processing by RNase P are tuned for uniform specificity and consequently optimal coupling to precursor biosynthesis
physiological function
the enzyme is an RNA-based enzyme primarily responsible for 5'-end pre-tRNA processing
physiological function
-
the enzyme is essential
physiological function
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the enzyme is required for the initial separation of all seven valine tRNAs from three distinct polycistronic transcripts, the processing of the seven valine tRNAs in Escherichia coli demands special features of the enzyme. Processing of the valU polycistronic transcript is completely dependent on RNase P. Processing of the lysT polycistronic operon requires RNase P but is stimulated by RNase E, EC 3.1.26.12
physiological function
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the enzyme RNase P is a tRNA processing enzyme. The enzyme can mediate inhibition of human cytomegalovirus gene expression and replication in U373MG cells, and the viral capsid formation, induced by engineered external guide sequences, overview. External guide sequences (EGSs) are RNA molecules that can bind to a target mRNA and direct ribonuclease P for specific cleavage of the target mRNA. Construction of EGS variants that efficiently direct human RNase P to cleave a target mRNA, coding for human cytomegalovirus capsid scaffolding protein and assemblin, in vitro. The EGS variant is about 40fold more active in directing human enzyme to cleave the mRNA in vitro than the EGS derived from a natural tRNA
physiological function
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the mutant enzyme variant is more effective in HIV RNA sequence cleavage and reducing HIV-1 p24 expression and intracellular viral RNA level in cells than the wild-type ribozyme. A reduction of about 90% in viral RNA level and a reduction of 150fold in viral growth are observed in human H9 cells that express the mutant, while a reduction of less than 10% is observed in H9 cells that either do not express the ribozyme or produce a catalytically inactive ribozyme mutant
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
physiological function
-
the principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts
physiological function
-
the ribonucleoprotein endoribonuclease is responsible for 5' maturation of precursor tRNA
physiological function
the enzyme is involved in maturation of the 5'-end of tRNA
physiological function
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maturation of tRNA depends on a single endonuclease, ribonuclease P, to remove highly variable 5' leader sequences from precursor tRNA transcripts
physiological function
the enzyme catalyzes 5'-end processing of tRNA
physiological function
the enzyme is involved in the 5' end processing of pre-tRNAs
physiological function
the enzyme is involved maturation of tRNAs by endonucleolytic cleavage of the pre-tRNA
physiological function
-
the enzyme removes the 5'-leader sequence from tRNA precursors
physiological function
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RNase P catalyzes 5'-maturation of tRNAs. Recombinant Ostreococcus tauri RPP can functionally reconstitute with bacterial RNase P RNAs but not with Ostreococcus tauri organellar RPRs, despite the latter's presumed bacterial origin
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physiological function
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the enzyme is involved maturation of tRNAs by endonucleolytic cleavage of the pre-tRNA
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physiological function
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the enzyme is involved in the 5' end processing of pre-tRNAs
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physiological function
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the enzyme is required for the initial separation of all seven valine tRNAs from three distinct polycistronic transcripts, the processing of the seven valine tRNAs in Escherichia coli demands special features of the enzyme. Processing of the valU polycistronic transcript is completely dependent on RNase P. Processing of the lysT polycistronic operon requires RNase P but is stimulated by RNase E, EC 3.1.26.12
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physiological function
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the stem loops of the RNase P RNA are required as binding sites for the proteins, their interactions are predominantly involved in stabilizing the active conformation of the enzyme
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physiological function
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the enzyme is involved in the procvessing of the leader sequence of precursor tRNA
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physiological function
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ribonuclease P is a ribonucleoprotein complex involved in the processing of the 5'-leader sequence of precursor tRNA (pre-tRNA). RNaseP proteins are predominantly involved in optimization of the pRNA conformation, though they are individually dispensable for RNase P activity in vitro
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additional information
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Arabidopsis thaliana PRORP1 can replace the bacterial ribonucleoprotein RNase P in Escherichia coli cells
additional information
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in bacteria, RNase P is composed of a catalytic RNA, PRNA, and a protein subunit, P protein, necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
additional information
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RNas P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview. Ab initio modeling fails to define unique scattering envelopes
additional information
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RNas P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview. Ab initio modeling fails to define unique scattering envelopes
additional information
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RNas P RNA solution structure determination using small angle X-ray scattering and selective 29-hydroxyl acylation analyzed by primer extension, SHAPE, analysis, generation of all-atom RNA models, overview. Ab initio modeling fails to define unique scattering envelopes
additional information
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the catalytic RNP has an H1 RNA moiety associated with ten distinct protein subunits. Five out of eight of these protein subunits, Rpp20, Rpp21, Rpp25, Rpp29, and Pop5, prepared in refolded recombinant forms, bind to H1 RNA in vitro. Rpp20 and Rpp25 bind jointly to H1 RNA, even though each protein can interact independently with this transcript. Nuclease footprinting analysis reveals that Rpp20 and Rpp25 recognize overlapping regions in the P2 and P3 domains of H1 RNA. Rpp21 and Rpp29, which are sufficient for reconstitution of the endonucleolytic activity, bind to separate regions in the catalytic domain of H1 RNA, subunit binding site analysis on H1 RNA, overview
additional information
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the Pyrobaculum sp. RNase P RNA is about 50% smaller compared to other archaeal RNase Ps
additional information
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all existing bacterial versions of the rnpA sequence might retain the elements required for functional interaction with the RNase P RNA. But the similarity of the heterologue to the endogenous version does not predict the fitness costs of the replacement
additional information
Arabidopsis thaliana contains a protein only form of RNase P, modeling of PRORP-tRNA interaction
additional information
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Arabidopsis thaliana contains a protein only form of RNase P, modeling of PRORP-tRNA interaction
additional information
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in bacteria, RNase P is composed of a catalytic RNA and a protein subunit (P protein) necessary for function in vivo. The P protein enhances pre-tRNA affinity, selectivity, and cleavage efficiency, as well as modulates the cation requirement for RNase P function. The two residues R60 and R62 in the most highly conserved region of the P protein, the RNR motif formed by residues R60-R68, stabilize PRNA complexes with both P protein and pre-tRNA, overview. The RNR motif enhances a metal-stabilized conformational change in RNase P that accompanies substrate binding and is essential for efficient catalysis
additional information
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in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit (P RNA, 350-400 nt) and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve effi cient RNA-alone catalysis
additional information
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in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve efficient RNA-alone catalysis
additional information
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in bacteria, the enzyme is a ribonucleoprotein composed of two essential subunits: a catalytic RNA subunit and a single small protein cofactor, P protein, secondary structure and tertiary interactions, overview. The RNA subunit of bacterial RNase P is an efficient catalyst in vitro in the absence of its single protein cofactor, while the protein cofactor is essential for RNase P function in vivo, affecting the structure, function, and kinetics of the holoenzyme under physiological salt conditions. In vitro, the protein subunit is dispensable, but its absence has to be compensated for by increased mono- and particularly divalent cations in order to achieve efficient RNA-alone catalysis
additional information
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in plants, the protein Pop1p is associated with MRP RNAs, i.e. mitochondrial RNA processing RNAs which cleave the large rRNA precursor at the A3 site, and with the catalytic subunit of enzyme RNase P, either separately or in a single large complex. Pop1p-specific antibodies precipitate RNase P activity from wheat extracts. The eukaryotic RNase P consensus sequence with CR II and CR III that are signature elements specific for RNase P RNA
additional information
L0N807
in plants, the protein Pop1p is associated with MRP RNAs, i.e. mitochondrial RNA processing RNAs which cleave the large rRNA precursor at the A3 site, and with the catalytic subunit of enzyme RNase P, either separately or in a single large complex. The eukaryotic RNase P consensus sequence with CR II and CR III that are signature elements specific for RNase P RNA
additional information
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modeling of RNP-based RNase P
additional information
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modeling of RNP-based RNase P
additional information
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modeling of RNP-based RNase P
additional information
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modeling of RNP-based RNase P
additional information
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modeling of RNP-based RNase P
additional information
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RNase P-mediated inhibition of gene expression represents a novel and promising nucleic acid-based gene interference strategy for specific inhibition of target mRNA, overview
additional information
structure-function analysis of proteinaceous RNase P, i.e. the enzyme consisting of only a protein part without catalytic RNA. The anticodon domain of transfer RNA is dispensable, whereas individual residues in D and TpsiC loops are essential for enzyme function, enzyme/transfer RNA interaction, mode of action of the proteinaceous enzyme, overview. Transfer RNA recognition by the proteinaceous PRORP enzyme is similar to that by ribonucleoprotein RNase P enzyme
additional information
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the enzyme is a ribonlucleoprotein, the RNAsubunit, termed P RNA, contains the active site, whereas the smaller protein subunit is required for optimal molecular recognition and catalysis in vitro and is essential in vivo
additional information
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the enzyme is a ribonucleoprotein consisting of one protein and one RNA subunit, referred to as C5 and RNase P RNA, respectively. The RNase P RNA is composed of domains that have different functions, the structural architecture of the -1/+73 plays a significant role where a C-1/G+73 pair has the most dramatic effect on kobs
additional information
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the enzyme is composed of RNA and five proteins (UniProtIDs: O59425, O59150, O59543, and O59248), the proteins assists the RNA part in attaining a functionally active conformation via a distinct mode of binding. Three archaeal proteins, PhoPop5, PhoRpp29, and PhoRpp30, are capable of promoting both, RNA annealing and displacement activities. They function as RNA chaperones or RNA annealers, fluorescence spectrometric analysis, overview. Protein PhoRpp21 shows low activity as annealer, and proein PhoRpp38 is inactive in annealing and strand displacement
additional information
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the enzyme is composed of two proteins, which localize to the nucleus and the mitochondrion, respectively, and have RNase P activity each on their own. The proteins PRORP1 and PRORP2 are the sole forms of RNase P in trypanosomatids
additional information
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the metal-dependent conformational change re-organizes the bound substrate in the active site to form a catalytically competent RNase P-pre-tRNA complex
additional information
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the organellar RNase P RNAs are expressed in vivo, however under in vitro conditions, catalysis of pre-tRNA cleavage is not observed even when associated with the nuclear encoded bacterial-like protein. Modeling of PRORP-tRNA interaction and RNP-based RNase P
additional information
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the two protein subunits StPop5 and StRpp25 are associated with with floral bud enzyme activity but not with leaf enzyme activity
additional information
wild-type and mutant enzyme structure-function analysis, overview. RNA U52 and two bacterially conserved protein residues, F17 and R89, are essential for efficient Thermotoga maritima enzyme activity. The U52 nucleotide binds a metal ion at the active site, whereas F17 and R89 are positioned over 20 A from the cleavage site, probably making contacts with N-4 and N-5 nucleotides of the pretRNA 5'-leader
additional information
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wild-type and mutant enzyme structure-function analysis, overview. RNA U52 and two bacterially conserved protein residues, F17 and R89, are essential for efficient Thermotoga maritima enzyme activity. The U52 nucleotide binds a metal ion at the active site, whereas F17 and R89 are positioned over 20 A from the cleavage site, probably making contacts with N-4 and N-5 nucleotides of the pretRNA 5'-leader
additional information
the secondary structure of RNase P RNA is reexamined using stringent comparative tools to arrive at phylogenetically supported model. The model structure shows an essentially flat disk with 16 tightly packed helices and a conserved face suitable for the binding of pre-tRNA. The low resolution model derived from small-angle X-ray scattering and the comparative 3-D model have similar overall shapes. The 3-D model provides a framework for a better understanding of structure-function relationships of this multifaceted primordial ribozyme