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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Apr;62(4):1229–1236. doi: 10.1073/pnas.62.4.1229

LEUCINE tRNA AND CESSATION OF Escherichia coli PROTEIN SYNTHESIS UPON PHAGE T2 INFECTION*

Tamiko Kano-Sueoka 1,2, Noboru Sueoka 1,2
PMCID: PMC223638  PMID: 4894692

Abstract

The involvement of tRNA in cellular differentiation has been tested by analyzing aminoacyl-tRNA of Escherichia coli after phage T2 infection. One or two minutes after infection, half of one of the five leucine tRNA components (Leu-tRNA1, CUG responding) undergoes a drastic structural change which leads to inactivity of both leucine acceptor activity and codon response. Whether or not the modification causes cessation of host protein synthesis without inhibiting phage-specific protein synthesis has been examined by analyzing polysome-bound leucine tRNA of E. coli before and after the phage infection. The results presented in this paper indicate that the amount of Leu-tRNA1 used after infection was greatly reduced as compared to that used in noninfected cells. Studies of the in vitro protein-synthesizing system show that T2 mRNA rarely contains the CUG codon. A mechanism by which host mRNA translation is inhibited by the phage infection is proposed from this available information.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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