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Literature summary for 3.1.26.5 extracted from

  • Marvin, M.C.; Engelke, D.R.
    RNase P: increased versatility through protein complexity? (2009), RNA Biol., 6, 40-42.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Saccharomyces cerevisiae 5737
-
mitochondrion
-
 Homo sapiens 5739
-
mitochondrion
-
 Saccharomyces cerevisiae 5739
-
nucleus
-
 Saccharomyces cerevisiae 5634
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-rRNA + H2O RNase MRP is involved with the maturation of pre-rRNA but cleaves RNA primers in mitochondria and localizes to cytoplasmic P-bodies where it takes part in cell cycle-regulated turnover of selected mRNAs Saccharomyces cerevisiae ?
-
 ?
pre-tRNA + H2O
-
 Saccharomyces cerevisiae ?
-
 ?
pre-tRNA + H2O in mitochondria, RNase P function has been taken over by an unrelated, protein-only enzyme activity Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
ribonuclease P
-
 Homo sapiens
ribonuclease P
-
 Saccharomyces cerevisiae
RNase MRP
-
 Saccharomyces cerevisiae
RNase P
-
 Homo sapiens
RNase P
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function 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 Saccharomyces cerevisiae