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Synonyms
rnase p, rnase p rna, rnase mrp, ribonuclease p, m1 rna, c5 protein, rnase p protein, rnase p holoenzyme, rpp30, protein c5,
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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
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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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 plays a role in precursor tRNA processing
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
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oligomer
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a multi-subunit catalytic ribonucleoprotein complex. Step-wise, Mg2+-dependent reconstitutions of Pfu RNaseP with its catalytic RNA subunit and two interacting protein cofactor pairs (RPP21/RPP29 and POP5/RPP30) reveals functional RNP intermediates en route to the RNaseP enzyme 1:1 composition for all subunits when either one or both protein complexes bind the cognate RNA
oligomer
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the archaeal holoenzyme is associated with 1 RNase P RNA and at least 4 RNase P proteins (POP5, RPP30, RPP21 and RPP29). Archaeal RNase P proteins function as two binary RNase P protein complexes (POP5/RPP30 and RPP21/RPP29). Archaeal POP5/RPP30 reconstituted with bacterial and organellar RNase P RNAs. While POP5/RPP30 is solely responsible for enhancing the cleavage rate of precursor tRNA by RNase P RNAs (by 60fold), RPP21/RPP29 contributes to increased substrate affinity (by 16-fold)
oligomer
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the RNA-binding protein L7Ae (UniProt: Q8U160) is a subunit of the archaeal RNase P ribonucleoprotein complex. The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA
additional information
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RNase P contains an essential RNase P RNA and RNase P protein
additional information
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archaeal RNase P comprises a catalytic RNase P RNA, RPR, and at least four protein cofactors, RPPs, which function as two binary complexes, POP5/RPP30 and RPP21/RPP29
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A14V
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RPP21 mutant, wild-type RPP21 binds to RPP29 3fold tighter than the mutant
C71V
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the single-Cys substitutions are introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein. The C71V parental reference is more active than the wild type enzyme
K42C
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mutation does not affect activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
R46C
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mutation results in 28% decrease in activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
V95C
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mutation results in 6% decrease in activity. The single-Cys substitution is introduced into a Cys-less Pfu L7Ae template C71V (i.e. RNA-binding protein L7Ae, subunit of archaeal RNase P). The native C71, which is partly buried, is mutated to Val to preserve the native fold and hydrophobic core of the protein
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Wilson, R.C.; Bohlen, C.J.; Foster, M.P.; Bell, C.E.
Structure of Pfu Pop5, an archaeal RNase P protein
Proc. Natl. Acad. Sci. USA
103
873-878
2006
Pyrococcus furiosus (Q8U151)
brenda
Kawamoto, S.A.; Sudhahar, C.G.; Hatfield, C.L.; Sun, J.; Behrman, E.J.; Gopalan, V.
Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives
Nucleic Acids Res.
36
697-704
2008
Escherichia coli, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Pyrococcus furiosus
brenda
Tsai, H.Y.; Pulukkunat, D.K.; Woznick, W.K.; Gopalan, V.
Functional reconstitution and characterization of Pyrococcus furiosus RNase P
Proc. Natl. Acad. Sci. USA
103
16147-16152
2006
Pyrococcus furiosus
brenda
Amero, C.D.; Boomershine, W.P.; Xu, Y.; Foster, M.
Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner
Biochemistry
47
11704-11710
2008
Pyrococcus furiosus (Q8U0H6), Pyrococcus furiosus
brenda
Xu, Y.; Amero, C.D.; Pulukkunat, D.K.; Gopalan, V.; Foster, M.P.
Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA in
J. Mol. Biol.
393
1043-1055
2009
Methanocaldococcus jannaschii, Pyrococcus furiosus
brenda
Cho, I.M.; Kazakov, S.A.; Gopalan, V.
Evidence for recycling of external guide sequences during cleavage of bipartite substrates in vitro by reconstituted archaeal RNase P
J. Mol. Biol.
405
1121-1127
2011
Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanococcus maripaludis, Pyrococcus furiosus
brenda
Jarrous, N.; Gopalan, V.
Archaeal/eukaryal RNase P: subunits, functions and RNA diversification
Nucleic Acids Res.
38
7885-7894
2010
Saccharomyces cerevisiae, [Candida] glabrata, Escherichia coli, Homo sapiens, Methanothermobacter thermautotrophicus, Mus musculus, Mycoplasmopsis fermentans, Pyrococcus furiosus, Saccharolobus solfataricus
brenda
Sinapah, S.; Wu, S.; Chen, Y.; Pettersson, B.M.; Gopalan, V.; Kirsebom, L.A.
Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection
Nucleic Acids Res.
39
1105-1116
2011
Pyrococcus furiosus
brenda
Ma, X.; Lai, L.B.; Lai, S.M.; Tanimoto, A.; Foster, M.P.; Wysocki, V.H.; Gopalan, V.
Uncovering the stoichiometry of Pyrococcus furiosus RNase P, a multi-subunit catalytic ribonucleoprotein complex, by surface-induced dissociation and Ion mobility mass spectrometry
Angew. Chem. Int. Ed. Engl.
53
11483-11487
2014
Pyrococcus furiosus
brenda
Chen, W.Y.; Pulukkunat, D.K.; Cho, I.M.; Tsai, H.Y.; Gopalan, V.
Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex
Nucleic Acids Res.
38
8316-8327
2010
Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Pyrococcus furiosus
brenda
Lai, S.M.; Lai, L.B.; Foster, M.P.; Gopalan, V.
The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA
Nucleic Acids Res.
42
13328-13338
2014
Pyrococcus furiosus
brenda