Abstract
The carboxyl-terminal domain of colicin E5 was shown to inhibit protein synthesis of Escherichia coli. Its target, as revealed through in vivo and in vitro experiments, was not ribosomes as in the case of E3, but the transfer RNAs (tRNAs) for Tyr, His, Asn, and Asp, which contain a modified base, queuine, at the wobble position of each anticodon. The E5 carboxyl-terminal domain hydrolyzed these tRNAs just on the 3' side of this nucleotide. Tight correlation was observed between the toxicity of E5 and the cleavage of intracellular tRNAs of this group, implying that these tRNAs are the primary targets of colicin E5.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anticodon / metabolism*
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Bacterial Proteins / biosynthesis
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Bacterial Proteins / genetics
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Bacterial Proteins / pharmacology
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Base Sequence
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Cloning, Molecular
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Colicins / genetics
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Colicins / metabolism*
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Colicins / pharmacology
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Escherichia coli / drug effects
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Escherichia coli / metabolism
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Escherichia coli Proteins*
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Guanine / analogs & derivatives
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Guanine / analysis
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Molecular Sequence Data
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RNA, Bacterial / chemistry
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RNA, Bacterial / metabolism*
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RNA, Ribosomal, 16S / metabolism
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RNA, Transfer, Amino Acid-Specific / chemistry
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RNA, Transfer, Amino Acid-Specific / metabolism*
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RNA, Transfer, Asn / chemistry
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RNA, Transfer, Asn / metabolism
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RNA, Transfer, Asp / chemistry
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RNA, Transfer, Asp / metabolism
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RNA, Transfer, His / chemistry
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RNA, Transfer, His / metabolism
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RNA, Transfer, Tyr / chemistry
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RNA, Transfer, Tyr / metabolism
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Ribonucleases / genetics
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Ribonucleases / metabolism*
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Ribonucleases / pharmacology
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Ribosomes / metabolism
Substances
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Anticodon
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Bacterial Proteins
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Colicins
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Escherichia coli Proteins
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RNA, Bacterial
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RNA, Ribosomal, 16S
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RNA, Transfer, Amino Acid-Specific
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RNA, Transfer, Asn
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RNA, Transfer, Asp
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RNA, Transfer, His
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RNA, Transfer, Tyr
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ceiC protein, E coli
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colicin immunity proteins
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Guanine
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queuine
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Ribonucleases