title: Ribonuclease H: from discovery to 3D structure.
abstract: Ribonucleases H (RNases H) from Escherichia coli and retroviruses share common features at the primary amino acid sequence and activity levels. RNase H is involved in selection of the origins of replication in E. coli and in DNA synthesis of the positive strand of retroviruses. Crystallographic studies of E. coli RNase H indicate that several amino acids, conserved in both cellular and retroviral RNases H, form an active site for hydrolysis of the RNA of RNA-DNA hybrids. Multiple forms of RNase H are present in both prokaryotes and eukaryotes. It is suggested that these RNases H may be part of larger polypeptides and, as has been shown for reverse transcriptase RNase H derived from retroviruses, that the location and/or activity of the RNase H may be influenced by other regions of the polypeptides.
authors.affiliation: Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
authors.forename: R J
authors.initials: RJ
authors.lastname: Crouch
mesh_terms: D000595:Amino Acid Sequence; D004261:DNA Replication; D004722:Endoribonucleases / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D004926:Escherichia coli / Q000201:enzymology; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009154:Mutation; D016914:Ribonuclease H; D014779:Virus Replication
chemical_list: D004722:Endoribonucleases; D016914:Ribonuclease H