ArticleNucleic acids research2014
Crystal structure of RNase H3-substrate complex reveals parallel evolution of RNA/DNA hybrid recognition.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Genome-wide in vivo and ex vivo mapping of R-loops using engineered N-terminal hybrid-binding domain of RNase H3 (enDR3).Nucleic acids research · 2025Article
- Molecular details of the CPSF73-CPSF100 C-terminal heterodimer and interaction with Symplekin.Open biology · 2023Article
- Structural basis of R-loop recognition by the S9.6 monoclonal antibody.Nature communications · 2022Article
- RNase H is an exo- and endoribonuclease with asymmetric directionality, depending on the binding mode to the structural variants of RNA:DNA hybrids.Nucleic acids research · 2022Article
- The catalytic mechanism, metal dependence, substrate specificity, and biodiversity of ribonuclease H.Frontiers in microbiology · 2022Review
- Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.Journal of structural biology: X · 2022Review
- Alternative dimerization is required for activity and inhibition of the HEPN ribonuclease RnlA.Nucleic acids research · 2021Article
- RNase H2-RED carpets the path to eukaryotic RNase H2 functions.DNA repair · 2019Review
- Human proteins that interact with RNA/DNA hybrids.Genome research · 2018Article
- Division of labor among Mycobacterium smegmatis RNase H enzymes: RNase H1 activity of RnhA or RnhC is essential for growth whereas RnhB and RnhA guard against killing by hydrogen peroxide in stationary phase.Nucleic acids research · 2017Article
- Biochemical Characterization of Mycobacterium smegmatis RnhC (MSMEG_4305), a Bifunctional Enzyme Composed of Autonomous N-Terminal Type I RNase H and C-Terminal Acid Phosphatase Domains.Journal of bacteriology · 2015Article
- Enzymatic Activities of RNase H Domains of HIV-1 Reverse Transcriptase with Substrate Binding Domains of Bacterial RNases H1 and H2.Molecular biotechnology · 2015Article
- Ribonucleotides in bacterial DNA.Critical reviews in biochemistry and molecular biology · 2015Review
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2 authors.
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Abstract
RNases H participate in the replication and maintenance of genomic DNA. RNase H1 cleaves the RNA strand of RNA/DNA hybrids, and RNase H2 in addition hydrolyzes the RNA residue of RNA-DNA junctions. RNase H3 is structurally closely related to RNases H2, but its biochemical properties are similar to type 1 enzymes. Its unique N-terminal substrate-binding domain (N-domain) is related to TATA-binding protein. Here, we report the first crystal structure of RNase H3 in complex with its RNA/DNA substrate. Just like RNases H1, type 3 enzyme recognizes the 2'-OH groups of the RNA strand and detects the DNA strand by binding a phosphate group and inducing B-form conformation. Moreover, the N-domain recognizes RNA and DNA in a manner that is highly similar to the hybrid-binding domain of RNases H1. Our structure demonstrates a remarkable example of parallel evolution of the elements used in the specific recognition of RNA and DNA.
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