Peptidyl‐tRNA hydrolase is involved in lambda inhibition of host protein synthesis.

摘要: Escherichia coli rap mutants do not support vegetative growth of bacteriophage lambda and die upon transcription DNA bar sites. Bacteria harbouring a pth(ts) mutation synthesize thermosensitive peptidyl-tRNA hydrolase (Pth) at 42 degrees C from defect in protein synthesis. We present evidence that both mutations affect the same gene: (i) activity was found to be defective mutants; (ii) threshold temperature, pth cells, like mutants, prevented were killed by cloned sites; (iii) sequencing 1600 bp fragment comprising loci revealed an ORF located within limits set complementation analysis encoding putative polypeptide 21 kDa; (iv) cloning mutant DNAs single nucleotide transitions wild type sequence, resulting Arg134 His Gly101 Asp changes respectively. Analysis plasmid-directed proteins identified approximately N-terminal amino acid composition isoelectric point this match those expected sequence. propose Pth activity, directly or indirectly, is target for RNA leading cell death.