Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Bacteriophage T4 / genetics
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Bacteriophage T4 / metabolism*
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DNA Restriction-Modification Enzymes*
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Escherichia coli / metabolism
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Escherichia coli / virology
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Escherichia coli Proteins*
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RNA, Transfer, Lys / metabolism
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Ribonucleases / genetics*
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Ribonucleases / metabolism*
Substances
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Bacterial Proteins
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DNA Restriction-Modification Enzymes
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Escherichia coli Proteins
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RNA, Transfer, Lys
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HsdM protein, Bacteria
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PrrC protein, E coli
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Ribonucleases
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anticodon nuclease