Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.26.5 extracted from

  • Lai, L.B.; Bernal-Bayard, P.; Mohannath, G.; Lai, S.M.; Gopalan, V.; Vioque, A.
    A functional RNase P protein subunit of bacterial origin in some eukaryotes (2011), Mol. Genet. Genomics, 286, 359-369.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, in vitro transcription, and overexpression in Escherichia coli strain BL21(DE3) Ostreococcus tauri

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus a nuclear-encoded bacterial RNase P protein homologue Ostreococcus tauri 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Ostreococcus tauri

Organism

Organism UniProt Comment Textmining
Ostreococcus tauri Q00XA5 component RNPA
-
Ostreococcus tauri RCC745 Q00XA5 component RNPA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by cation exchange and metal chelating affinity chromatography Ostreococcus tauri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-tRNALeu + H2O
-
Ostreococcus tauri tRNALeu + 5' leader of tRNA
-
?
pre-tRNALeu + H2O
-
Ostreococcus tauri RCC745 tRNALeu + 5' leader of tRNA
-
?

Synonyms

Synonyms Comment Organism
RNase P
-
Ostreococcus tauri
RNase P protein
-
Ostreococcus tauri
RPP
-
Ostreococcus tauri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Ostreococcus tauri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Ostreococcus tauri

General Information

General Information Comment Organism
evolution comparison of nuclear, mitochondrial, and plastidic RPPs, overview Ostreococcus tauri
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 Ostreococcus tauri