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Literature summary for 3.1.26.5 extracted from

  • Marvin, M.C.; Walker, S.C.; Fierke, C.A.; Engelke, D.R.
    Binding and cleavage of unstructured RNA by nuclear RNase P (2011), RNA, 17, 1429-1440.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Inhibitors

Inhibitors Comment Organism Structure
mixed-sequence RNAs only a small fraction of the mixed-sequence RNA is cleaved by RNase P Saccharomyces cerevisiae
poly(U) RNA binding and structure analysis, overview Saccharomyces cerevisiae
unstructured, single-stranded RNA inhibits RNase P in a size-dependent manner, binding and structure analysis, overview Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
 Saccharomyces cerevisiae 5634
-

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information only a small fraction of the mixed-sequence RNA is cleaved by RNase P. Binding and cleavage of unstructured RNA by nuclear RNase P, overview Saccharomyces cerevisiae ?
-
 ?
pre-tRNATyr + H2O
-
 Saccharomyces cerevisiae tRNATyr + 5' leader of tRNA
-
 ?

Synonyms

Synonyms Comment Organism
RNase P
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function RNase P is an essential endoribonuclease processing the 59 leader of pre-tRNAs. Compared to bacterial RNase P, which contains a single small protein subunit and a large catalytic RNA subunit, eukaryotic nuclear RNase P is more complex, containing nine proteins and an RNA subunit in Saccharomyces cerevisiae. Nuclear RNase P has been shown to possess unique RNA binding capabilities, molecular recognition of nuclear RNase P, overview. Multiple interactions are required for high affinity binding Saccharomyces cerevisiae