Leucine tRNA and cessation of Escherichia coli protein synthesis upon phage T2 infection.
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.
D001426:Bacterial Proteins / Q000096:biosynthesis*; D002247:Carbon Isotopes; D002454:Cell Differentiation; D002845:Chromatography; D003090:Coliphages; D004926:Escherichia coli / Q000378:metabolism; D005815:Genetic Code; D007930:Leucine; D012333:RNA, Messenger; D012343:RNA, Transfer; D012270:Ribosomes / Q000378:metabolism; D014316:Tritium
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D012333:RNA, Messenger; D014316:Tritium; D012343:RNA, Transfer; D007930:Leucine