ArticleJournal of biochemistry2017
Effects of neutral salts and pH on the activity and stability of human RNase H2.
Article in Journal of biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
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- Comparative evaluation of ACetic - MEthanol high salt dissociation approach for single-cell transcriptomics of frozen human tissues.Frontiers in cell and developmental biology · 2024Article
- Programmable RNA targeting with CRISPR-Cas13.RNA biology · 2024Review
- A Method for Isolation Bacteriophage Particles-Free Genomic DNA, Exemplified by TP-84, Infecting ThermophilicMicroorganisms · 2022Article
- Val143 of human ribonuclease H2 is not critical for, but plays a role in determining catalytic activity and substrate specificity.PloS one · 2020Article
- Characterization of six recombinant human RNase H2 bearing Aicardi-Goutiéres syndrome causing mutations.Journal of biochemistry · 2019Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Ribonuclease H (RNase H) specifically degrades the RNA of RNA/DNA hybrid. Recent study has shown that a single ribonucleotide is embedded in DNA double strand at every few thousand base pairs in human genome, and human RNase H2 is involved in its removal. Here, we examined the effects of neutral salts and pH on the activity and stability of human RNase H2. NaCl, KCl, RbCl and NaBr increased the activity to 170-390% at 10-60 mM, while LiCl, LiBr and CsCl inhibited it, suggesting that species of cation, but not anion, is responsible for the effect on activity. NaCl and KCl increased the stability by decreasing the first-order rate constant of the inactivation to 50-60% at 60-80 mM. The activity at 25-35 °C exhibited a narrow bell-shaped pH-dependence with the acidic and alkaline pKe (pKe1 and pKe2) values of 7.3 - 7.6 and 8.1 - 8.8, respectively. Enthalpy changes (ΔH°) of deprotonation were 5 ± 21 kJ mol-1 for pKe1 and 68 ± 25 kJ mol-1 for pKe2. These results suggest that the ionizable groups responsible for pKe1 may be two out of Asp34, Glu35 and Asp141 of DEDD motif, and that for pKe2 may be Lys69 of DSK motif.
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