Release of ribosome bound transfer RNA by enzymatic digestion of messenger RNA

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Abstract

A factor other than G factor, which releases tRNA specific for phenylalanine (tRNAPhe) from the complex of ribosomes and polyuridylic acid has been purified and identified as either polynucleotide phosphorylase or ribonuclease II. The release is specific for unesterified tRNAPhe, and phenylalanyl-tRNA could not be released by digestion of polyuridylic acid. This is because phenylalanyl-tRNA, but not unesterified tRNAPhe, protects the ribosome-bound polyuridylic acid from digestion by these enzymes. Dissociation of ribosomes in the presence of the initiation factor (F3) does not take place if the ribosome contains bound tRNA. When tRNAPhe is removed from the ribosomal complex by ribonuclease II, through its digestion of polyuridylic acid, the initiation factor (F3) dissociates the 70-S ribosomes into 50-S and 30-S ribosomal subunits. tRNA, released from the ribosomal complex by these enzymes, retained its capacity to accept amino acid.

References (29)

  • H. Ishitsuka et al.

    J. Biol. Chem.

    (1970)
  • P.F. Spahr et al.

    J. Biol. Chem.

    (1963)
  • D.P. Fan et al.

    J. Mol. Biol.

    (1964)
  • J.J. Castles et al.

    J. Mol. Biol.

    (1969)
  • K. Momose et al.

    Arch. Biochem. Biophys.

    (1965)
  • A-L. Haenni et al.

    Biochim. Biophys. Acta

    (1966)
  • M.R. Lamborg et al.

    Biochem. Biophys. Res. Commun.

    (1965)
  • H. Kaji et al.

    Biochim. Biophys. Acta

    (1967)
  • R.W. Kohler et al.

    J. Mol. Biol.

    (1968)
  • G. Mangiarotti et al.

    J. Mol. Biol.

    (1966)
  • O.H. Lowry et al.

    J. Biol. Chem.

    (1951)
  • P. Leder et al.

    Biochem. Biophys. Res. Commun.

    (1966)
  • M.N. Thang et al.

    J. Mol. Biol.

    (1970)
  • H. Ishitsuka et al.
  • Cited by (6)

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