ArticleThe Journal of biological chemistry2010
The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 53 citations in OpenAlex.
- Emerging roles of RNA:DNA hybrid regulation by mammalian ribonuclease H2 in replication stress and cancer.Journal of cell science · 2025Review
- Distinct features of ribonucleotides within genomic DNA in Aicardi-Goutières syndrome ortholog mutants ofiScience · 2024Article
- Distinct features of ribonucleotides within genomic DNA in Aicardi-Goutières syndrome (AGS)-ortholog mutants ofbioRxiv : the preprint server for biology · 2023Article
- Development of an RNase H2 Activity Assay for Clinical Screening.Journal of clinical medicine · 2023Article
- The catalytic mechanism, metal dependence, substrate specificity, and biodiversity of ribonuclease H.Frontiers in microbiology · 2022Review
- 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
- Large-Scale Photolithographic Synthesis of Chimeric DNA/RNA Hairpin Microarrays To Explore Sequence Specificity Landscapes of RNase HII Cleavage.Biochemistry · 2019Article
- Aicardi-Goutières syndrome gene Rnaseh2c is a metastasis susceptibility gene in breast cancer.PLoS genetics · 2019Article
- Effects of neutral salts and pH on the activity and stability of human RNase H2.Journal of biochemistry · 2017Article
- Structural studies of RFCEMBO reports · 2017Article
- Ribonucleotide incorporation by human DNA polymerase η impacts translesion synthesis and RNase H2 activity.Nucleic acids research · 2017Article
- The Balancing Act of Ribonucleotides in DNA.Trends in biochemical sciences · 2016Review
- The Yin and Yang of R-loop biology.Current opinion in cell biology · 2015Review
- Reduction of hRNase H2 activity in Aicardi-Goutières syndrome cells leads to replication stress and genome instability.Human molecular genetics · 2015Article
- Crystal structure of a TAF1-TAF7 complex in human transcription factor IID reveals a promoter binding module.Cell research · 2014Article
- Identification of host proteins interacting with the integrin-like A domain of Toxoplasma gondii micronemal protein MIC2 by yeast-two-hybrid screening.Parasites & vectors · 2014Article
- Aicardi-Goutières syndrome: clues from the RNase H2 knock-out mouse.Journal of molecular medicine (Berlin, Germany) · 2013Review
- Synonymous mutations in RNASEH2A create cryptic splice sites impairing RNase H2 enzyme function in Aicardi-Goutières syndrome.Human mutation · 2013Article
- RNase H2 roles in genome integrity revealed by unlinking its activities.Nucleic acids research · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The mammalian RNase H2 ribonuclease complex has a critical function in nucleic acid metabolism to prevent immune activation with likely roles in processing of RNA primers in Okazaki fragments during DNA replication, in removing ribonucleotides misinserted by DNA polymerases, and in eliminating RNA.DNA hybrids during cell death. Mammalian RNase H2 is a heterotrimeric complex of the RNase H2A, RNase H2B, and RNase H2C proteins that are all required for proper function and activity. Mutations in the human RNase H2 genes cause Aicardi-Goutières syndrome. We have determined the crystal structure of the three-protein mouse RNase H2 enzyme complex to better understand the molecular basis of RNase H2 dysfunction in human autoimmunity. The structure reveals the intimately interwoven architecture of RNase H2B and RNase H2C that interface with RNase H2A in a complex ideally suited for nucleic acid binding and hydrolysis coupled to protein-protein interaction motifs that could allow for efficient participation in multiple cellular functions. We have identified four conserved acidic residues in the active site that are necessary for activity and suggest a two-metal ion mechanism of catalysis for RNase H2. An Okazaki fragment has been modeled into the RNase H2 nucleic acid binding site providing insight into the recognition of RNA.DNA junctions by the RNase H2. Further structural and biochemical analyses show that some RNase H2 disease-causing mutations likely result in aberrant protein-protein interactions while the RNase H2A subunit-G37S mutation appears to distort the active site accounting for the demonstrated substrate specificity modification.
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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.