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      Escherichia coli tRNase Z can shut down growth probably by removing amino acids from aminoacyl-tRNAs.

      Genes to Cells

      Transcription, Genetic, Substrate Specificity, metabolism, RNA, Transfer, Amino Acyl, RNA Precursors, Nucleic Acid Conformation, Molecular Sequence Data, genetics, Escherichia coli Proteins, enzymology, Escherichia coli, Endoribonucleases, Base Sequence, Amino Acids

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          Abstract

          In most organisms, tRNase Z is considered to be essential for 3' processing of tRNA molecules. The Escherichia coli tRNase Z gene, however, appears to be dispensable under normal growth conditions, and its existence remained an enigma. Here we intensively examined various (pre-)tRNAs for good substrates of E. coli tRNase Z in vitro, and found that the enzyme can remove the 3' terminal CCA residues from mature tRNAs regardless of their nucleotide modifications. Furthermore, we discovered that E. coli tRNase Z, when sufficiently expressed in the cell, can shut down growth probably by removing amino acids from aminoacyl-tRNAs. We confirmed in vitro that E. coli tRNase Z exceptionally possesses the activity that cleaves off the 3' terminal residues charging an amino acid from an aminoacyl-tRNA molecule. The current data suggest that tRNase Z might help modulate a cell growth rate by repressing translation under some stressful conditions.

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          Journal
          10.1111/j.1365-2443.2008.01230.x
          18823332

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