Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis.

By M. Nowotny, S. Gaidamakov, R. Crouch, Wei Yang. Cell, 2005

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microPrimer: the biogenesis and function of microRNA (2005, background): “…structure of the PIWI domain closely resembles that of RNase H, the enzyme that cleaves the RNA strand of an RNA-DNA hybrid (Song et al., 2004; Nowotny et al., 2005), and both structural and biochemical studies have confirmed that Argonaute is the target-cleaving endonuclease of the RISC (Liu…”
Chemistry, structure and function of approved oligonucleotide therapeutics (2023, background): “An overlay of crystal structures of Bacillus halodurans RNase H bound to an RNA-DNA substrate duplex (162) and a DNA–DNA inhibitor duplex of the same length (218) shows that the groove widths and strand curvatures in the two duplexes differ distinctly (Figure 8C).”
The Streptococcus thermophilus CRISPR/Cas system provides immunity in Escherichia coli (2011, background): “The RuvC-like nuclease domain is identified in proteins that act on both DNA and RNA, including RNaseH, RuvC, and PIWI domain of Argonaut proteins (27).”