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Literature summary for 3.1.26.5 extracted from

  • Walczyk, D.; Goessringer, M.; Rossmanith, W.; Zatsepin, T.S.; Oretskaya, T.S.; Hartmann, R.K.
    Analysis of the cleavage mechanism by protein-only RNase P using precursor tRNA substrates with modifications at the cleavage site (2016), J. Mol. Biol., 428, 4917-4928 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana F4JKB6
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pre-tRNA-Gly precursor + H2O analysis of the kinetics and cleavage-site selection by PRORP3 using precursor tRNAs (pre-tRNAs) with individual modifications at the canonical cleavage site, with either Rp- or Sp-phosphorothioate, or 2'-deoxy, 2'-fluoro, 2'-amino, or 2'-O-methyl substitutions. A small but robust rescue effect of Sp-phosphorothioate-modified pre-tRNA is observed in the presence of thiophilic Cd2+ ions,-consistent with metal-ion coordination to the (pro-)Sp-oxygen during catalysis. Sp-phosphorothioate, 2'-deoxy, 2'-amino, and 2'-O-methyl modification redirected the cleavage mainly to the next unmodified phosphodiester in the 5'-direction. The 2'-OH substituent at nucleotide -1 is involved in an H-bonding acceptor function. In contrast to bacterial RNase P, AtPRORP3 is able to utilize the canonical and upstream cleavage site with similar efficiency (corresponding to reduced cleavage fidelity), and the two cleavage pathways appear less interdependent than in the bacterial RNAbased system Arabidopsis thaliana tRNA-Gly + 5'-oligoribonucleotide
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Synonyms

Synonyms Comment Organism
PRORP3
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Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
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assay at Arabidopsis thaliana