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Science 26 March 1999:
Vol. 283. no. 5410, pp. 2097 - 2100
DOI: 10.1126/science.283.5410.2097

Reports

A Cytotoxic Ribonuclease Targeting Specific Transfer RNA Anticodons

T. Ogawa, 1 K. Tomita, 2* T. Ueda, 2 K. Watanabe, 2 T. Uozumi, 1 H. Masaki 1dagger

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.

1 Department of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan.
2 Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-8654, Japan.
*   Present address: Institut de Biologie Moléculaire des Plantes du CNRS, 12 rue du Général Zimmer, F-67084, Strasbourg Cedex, France.

dagger    To whom correspondence should be addressed. E-mail: hmasaki{at}mcb.bt.a.u-tokyo.ac.jp


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