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Literature summary for 3.1.26.5 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)

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

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
-
-
-
Methanothermobacter thermautotrophicus
-
-
-
Pyrococcus furiosus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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
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

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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