PMID:2177653
| Citation |
Crouch, RJ (1990) Ribonuclease H: from discovery to 3D structure. New Biol. 2:771-7 |
|---|---|
| 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. |
| Links | |
| Keywords |
Amino Acid Sequence; DNA Replication; Endoribonucleases/chemistry; Endoribonucleases/genetics; Endoribonucleases/physiology; Escherichia coli/enzymology; Molecular Sequence Data; Molecular Structure; Mutation; Ribonuclease H; Virus Replication |
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