ArticleThe Journal of biological chemistry2011
The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutières syndrome defects.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 61 citations in OpenAlex.
- DNA damage induces long range changes to duplex structure-a non-protein start to damage detection?Nucleic acids research · 2026Article
- Ribonucleotide errors, RNase HII, and ribonucleotide excision repair.Critical reviews in biochemistry and molecular biology · 2026Review
- RNaseH2 inhibition potentiates temozolomide response in patient derived glioblastoma cells.Scientific reports · 2025Article
- Genome-wide DNA methylation analysis of CBCVd-infected hop plants (Microbiology spectrum · 2025Article
- Expanding the phenotypic spectrum ofCurrent journal of neurology · 2025Article
- The Smc5/6 complex counteracts R-loop formation at highly transcribed genes in cooperation with RNase H2.eLife · 2024Article
- Distinct features of ribonucleotides within genomic DNA in Aicardi-Goutières syndrome ortholog mutants ofiScience · 2024Article
- Development of an RNase H2 Activity Assay for Clinical Screening.Journal of clinical medicine · 2023Article
- Review
- RNase H2, mutated in Aicardi-Goutières syndrome, resolves co-transcriptional R-loops to prevent DNA breaks and inflammation.Nature communications · 2022Article
- DNA damage contributes to neurotoxic inflammation in Aicardi-Goutières syndrome astrocytes.The Journal of experimental medicine · 2022Article
- ADAR1 RNA editing enzyme regulates R-loop formation and genome stability at telomeres in cancer cells.Nature communications · 2021Article
- Case Report: Novel Compound HeterozygousFrontiers in immunology · 2021Article
- Novel alternative ribonucleotide excision repair pathways in human cells by DDX3X and specialized DNA polymerases.Nucleic acids research · 2020Article
- Impact of 1,The Journal of biological chemistry · 2020Article
- Molecular and physiological consequences of faulty eukaryotic ribonucleotide excision repair.The EMBO journal · 2020Review
- Val143 of human ribonuclease H2 is not critical for, but plays a role in determining catalytic activity and substrate specificity.PloS one · 2020Article
- Article
- Characterization of six recombinant human RNase H2 bearing Aicardi-Goutiéres syndrome causing mutations.Journal of biochemistry · 2019Article
- RNase H2-RED carpets the path to eukaryotic RNase H2 functions.DNA repair · 2019Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
RNase H2 cleaves RNA sequences that are part of RNA/DNA hybrids or that are incorporated into DNA, thus, preventing genomic instability and the accumulation of aberrant nucleic acid, which in humans induces Aicardi-Goutières syndrome, a severe autoimmune disorder. The 3.1 Å crystal structure of human RNase H2 presented here allowed us to map the positions of all 29 mutations found in Aicardi-Goutières syndrome patients, several of which were not visible in the previously reported mouse RNase H2. We propose the possible effects of these mutations on the protein stability and function. Bacterial and eukaryotic RNases H2 differ in composition and substrate specificity. Bacterial RNases H2 are monomeric proteins and homologs of the eukaryotic RNases H2 catalytic subunit, which in addition possesses two accessory proteins. The eukaryotic RNase H2 heterotrimeric complex recognizes RNA/DNA hybrids and (5')RNA-DNA(3')/DNA junction hybrids as substrates with similar efficiency, whereas bacterial RNases H2 are highly specialized in the recognition of the (5')RNA-DNA(3') junction and very poorly cleave RNA/DNA hybrids in the presence of Mg(2+) ions. Using the crystal structure of the Thermotoga maritima RNase H2-substrate complex, we modeled the human RNase H2-substrate complex and verified the model by mutational analysis. Our model indicates that the difference in substrate preference stems from the different position of the crucial tyrosine residue involved in substrate binding and recognition.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.