Leucine tRNA and cessation of Escherichia coli protein synthesis upon phage T2 infection.

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-tRNA(1), 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-tRNA(1) 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.

• Authors: T Kano-Sueoka, N Sueoka
• Journal: Proceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A) Vol. 62 Issue 4 Pg. 1229-36 (Apr 1969) ISSN: 0027-8424 [Print] United States
• PMID: 4894692 (Publication Type: Journal Article)

Chemical References

• Bacterial Proteins
• Carbon Isotopes
• RNA, Messenger
• Tritium
• RNA, Transfer
• Leucine

Topics

• Bacterial Proteins (biosynthesis)
• Carbon Isotopes
• Cell Differentiation
• Chromatography
• Coliphages
• Escherichia coli (metabolism)
• Genetic Code
• Leucine
• RNA, Messenger
• RNA, Transfer
• Ribosomes (metabolism)
• Tritium