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Literature summary extracted from

  • 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 (2010), Nucleic Acids Res., 38, 8316-8327.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.26.5
-
Methanothermobacter thermautotrophicus
3.1.26.5
-
Pyrococcus furiosus
3.1.26.5
-
Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.5 Methanocaldococcus jannaschii
-
-
-
3.1.26.5 Methanothermobacter thermautotrophicus
-
-
-
3.1.26.5 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.26.5
-
Methanothermobacter thermautotrophicus
3.1.26.5
-
Pyrococcus furiosus
3.1.26.5
-
Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.5 pre-tRNATyr + H2O pre-tRNATyr from Escherichia coli Methanothermobacter thermautotrophicus tRNATyr + 5'-oligoribonucleotide
-
?
3.1.26.5 pre-tRNATyr + H2O pre-tRNATyr from Escherichia coli Pyrococcus furiosus tRNATyr + 5'-oligoribonucleotide
-
?
3.1.26.5 pre-tRNATyr + H2O pre-tRNATyr from Escherichia coli Methanocaldococcus jannaschii tRNATyr + 5'-oligoribonucleotide
-
?

Subunits

EC Number Subunits Comment Organism
3.1.26.5 oligomer 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) Pyrococcus furiosus
3.1.26.5 oligomer 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 16fold) Methanothermobacter thermautotrophicus
3.1.26.5 oligomer 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 16fold) Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
3.1.26.5 RNase P
-
Methanothermobacter thermautotrophicus
3.1.26.5 RNase P
-
Pyrococcus furiosus
3.1.26.5 RNase P
-
Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.26.5 55
-
assay at Methanothermobacter thermautotrophicus
3.1.26.5 55
-
assay at Pyrococcus furiosus
3.1.26.5 55
-
assay at Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.26.5 7.5
-
assay at Methanothermobacter thermautotrophicus
3.1.26.5 7.5
-
assay at Pyrococcus furiosus
3.1.26.5 7.5
-
assay at Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
3.1.26.5 physiological function the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs Methanothermobacter thermautotrophicus
3.1.26.5 physiological function the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs Pyrococcus furiosus
3.1.26.5 physiological function the enzyme catalyzes the Mg2+-dependent 5'-maturation of precursor tRNAs Methanocaldococcus jannaschii