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Literature summary extracted from

  • Taschner, A.; Weber, C.; Buzet, A.; Hartmann, R.K.; Hartig, A.; Rossmanith, W.
    Nuclear RNase P of Trypanosoma brucei: a single protein in place of the multicomponent RNA-protein complex (2012), Cell Rep., 2, 19-25.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.26.5 genes PRORP1 and PRORP2, recombinant expression of C-terminally His6-tagged PRORP1 and of C-terminally His6-tagged and N-terminally GST-tagged PRORP2 in Escherichia coli Trypanosoma brucei

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.26.5 mitochondrion the enzyme is composed of two proteins, protein PRORP2 is localized to the branched trypanosomatid mitochondrion and has a cleavable N-terminal targeting sequence Trypanosoma brucei 5739
-
3.1.26.5 nucleolus the enzyme is composed of a catalytic RNA and two proteins, protein PRORP1 is largely confined to the single central nucleolus of the nuclei and only weak in the nucleoplasm Trypanosoma brucei 5730
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.26.5 70000
-
-
 Trypanosoma brucei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.26.5 additional information Trypanosoma brucei RNase P is the endonuclease that removes 5' extensions from tRNA precursors ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.5 Trypanosoma brucei
-
 genes PRORP1 and PRORP2
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.26.5 no ribonucleoprotein
-
 Trypanosoma brucei

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.26.5 recombinant C-terminally His6-tagged PRORP1 from Escherichia coli by nickel affinity chromatography, recombinant C-terminally His6-tagged and N-terminally GST-tagged PRORP2 from Escherichia coli by nickel and glutathione affinity chromatography, and proteolytical cleavage of the GST-tag, both proteins ar further purified by gel filtration Trypanosoma brucei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.5 additional information RNase P is the endonuclease that removes 5' extensions from tRNA precursors Trypanosoma brucei ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.26.5 PRORP
-
 Trypanosoma brucei
3.1.26.5 PRORP1
-
 Trypanosoma brucei
3.1.26.5 PRORP2
-
 Trypanosoma brucei
3.1.26.5 proteinaceous RNase P
-
 Trypanosoma brucei
3.1.26.5 RNase P
-
 Trypanosoma brucei

General Information

EC Number General Information Comment Organism
3.1.26.5 evolution in the evolved, modern RNase P enzymes, the RNA depends on protein to fulfill its cellular function. This RNA-based form of RNase P is found in all domains of life, but there is an apparent trend from RNA to protein predominance in the overall composition and functioning of these ribonucleoproteins from bacteria to eukarya. RNase P of the former is built from a catalytically proficient RNA and a single small protein only. RNase P RNA of Archaea is a less-efficient catalyst in vitro and associates with five proteins, none of which is related to the bacterial protein. Another entirely different form of RNase P, i.e. proteinaceous RNase P, apparently not containing RNA, is initially observed in the organelles of different eukarya, e.g. humans, and also in Trypanosoma brucei. The genomes of trypanosomatids lack evidence for genes related to RNA-based RNase P, but they encode two homologues of human and plant PRORP genes. Also in plants, all cellular tRNA 5' end maturation appears to be exclusively protein dependent Trypanosoma brucei
3.1.26.5 additional information the enzyme is composed of two proteins, which localize to the nucleus and the mitochondrion, respectively, and have RNase P activity each on their own. The proteins PRORP1 and PRORP2 are the sole forms of RNase P in trypanosomatids Trypanosoma brucei
3.1.26.5 physiological function RNase P is the endonuclease that removes 5' extensions from tRNA precursors, an early and essential step in tRNA biogenesis. PRORP1 Is able to substitute for Saccharomyces cerevisiae strain BY4743 nuclear RNase P in vivo, the inherently different physical qualities of the two enzyme forms are not reflected in a basically different functionality Trypanosoma brucei