Anticodon nucleases.
A tRNALys-specific anticodon nuclease is kept in a latent form in a rare Escherichia coli strain, complexed with a DNA restriction enzyme. A phage T4 inhibitor of DNA restriction activates anticodon nuclease, but other T4 proteins restore tRNALys. Detection of a homologous system in Neisseria and a different anticodon nuclease in colicin E5 suggest ubiquity and diversity of such tRNA toxins. Analysis of these systems could reveal novel RNA recognition and cleavage mechanisms.
Kaufmann
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Dept of Biochemistry, Tel Aviv University, Ramat Aviv 69978, Israel. kaufmann@post.tau.ac.il
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D017122:Bacteriophage T4 / Q000235:genetics / Q000378:metabolism*; D015280:DNA Restriction-Modification Enzymes; D004926:Escherichia coli / Q000378:metabolism / Q000821:virology; D029968:Escherichia coli Proteins; D012357:RNA, Transfer, Lys / Q000378:metabolism; D012260:Ribonucleases / Q000235:genetics* / Q000378:metabolism*
D001426:Bacterial Proteins; D015280:DNA Restriction-Modification Enzymes; D029968:Escherichia coli Proteins; D012357:RNA, Transfer, Lys; C109829:HsdM protein, Bacteria; C084965:PrrC protein, E coli; D012260:Ribonucleases; C049345:anticodon nuclease