Ribosome-inhibiting proteins, retroviral reverse transcriptases, and RNase H share common structural elements.
Plant ribosome-inhibiting proteins are shown to be homologous at the domain level to RNase H from Escherichia coli and to two regions of the pol gene product of retroviral reverse transcriptases. One of these regions carries the viral integrase or int function, while the other has previously been suggested to contain the viral RNase H exo activity. Several residues conserved among the ribosome inhibitors, E. coli RNase H, and the integrase proteins are seen to occupy a prominent cleft in the tertiary structure of the ribosome inhibitor ricin, suggesting roles in binding or catalysis. It is likely that these homologous sequences represent modern derivatives of an ancient protein-folding unit capable of nucleic acid binding and modification which has been incorporated into a variety of enzyme functions.
D000595:Amino Acid Sequence; D004722:Endoribonucleases; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins; D010944:Plants; D011487:Protein Conformation; D011500:Protein Synthesis Inhibitors; D012194:RNA-Directed DNA Polymerase; D012190:Retroviridae / Q000201:enzymology; D016914:Ribonuclease H; D012270:Ribosomes / Q000187:drug effects
D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D012194:RNA-Directed DNA Polymerase; D004722:Endoribonucleases; D016914:Ribonuclease H