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Literature summary extracted from

  • Cho, I.M.; Kazakov, S.A.; Gopalan, V.
    Evidence for recycling of external guide sequences during cleavage of bipartite substrates in vitro by reconstituted archaeal RNase P (2011), J. Mol. Biol., 405, 1121-1127.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.1.26.5 biotechnology RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs Methanothermobacter thermautotrophicus
3.1.26.5 biotechnology RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs Pyrococcus furiosus
3.1.26.5 biotechnology RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs Methanocaldococcus jannaschii
3.1.26.5 biotechnology RNA-mediated RNA cleavage events are being increasingly exploited to disrupt RNA function, an important objective in post-genomic biology. RNase P, a ribonucleoprotein enzyme that catalyzes the removal of 5'-leaders from precursor tRNAs, has previously been utilized for sequence-specific cleavage of cellular RNAs Methanococcus maripaludis

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.5 additional information an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro Methanothermobacter thermautotrophicus ?
-
 ?
3.1.26.5 additional information an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro Pyrococcus furiosus ?
-
 ?
3.1.26.5 additional information an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro Methanocaldococcus jannaschii ?
-
 ?
3.1.26.5 additional information an external guide sequence, EGS, RNA base-paired to a target RNA makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS complex a precursor tRNA structural mimic. RNase P holoenzymes recognize and cleave such substrate-EGS complexes. The external guide sequences engage in multiple rounds of substrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro Methanococcus maripaludis ?
-
 ?
3.1.26.5 pre-tRNA + H2O RNase P holoenzymes, reconstituted in vitro Methanothermobacter thermautotrophicus tRNA + 5' leader of tRNA
-
 ?
3.1.26.5 pre-tRNA + H2O RNase P holoenzymes, reconstituted in vitro Pyrococcus furiosus tRNA + 5' leader of tRNA
-
 ?
3.1.26.5 pre-tRNA + H2O RNase P holoenzymes, reconstituted in vitro Methanocaldococcus jannaschii tRNA + 5' leader of tRNA
-
 ?
3.1.26.5 pre-tRNA + H2O RNase P holoenzymes, reconstituted in vitro Methanococcus maripaludis tRNA + 5' leader of tRNA
-
 ?

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
3.1.26.5 RNase P
-
 Methanococcus maripaludis