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Science 26 March 1999: Vol. 283. no. 5410, pp. 2097 - 2100 DOI: 10.1126/science.283.5410.2097
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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
1
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.
To whom correspondence should be addressed. E-mail:
hmasaki{at}mcb.bt.a.u-tokyo.ac.jp
Read the Full Text
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