Suppression of amber mutations of bacteriophage T4 gene 43 (DNA polymerase) by translational ambiguity

J Virol. 1973 Jun;11(6):933-45. doi: 10.1128/JVI.11.6.933-945.1973.


The growth properties of twelve different amber (am) mutants of bacteriophage T4 gene 43 (DNA polymerase) were examined by using nonpermissive (su(-)) as well as permissive (su(+)) Escherichia coli hosts. It was found that most of these mutants were measurably suppressed in su(-) hosts by translational ambiguity (misreading of codons during protein synthesis). The ability of these mutants to grow in response to this form of weak suppression probably means that the T4 gene 43 DNA polymerase can be effective in supporting productive DNA replication when it is supplied in small amounts. By similar criteria, studies with other phage mutants suggested that the products of T4 genes 62 (uncharacterized), 44 (uncharacterized), 42 (dCMP-hydroxymethylase), and 56 (dCTPase) are also effective in small amounts. Some T4 gene products, such as the product of gene 41 (uncharacterized), seem to be partially dispensable for phage growth since am mutants of such genes do propagate, although weakly, in streptomycin-resistant su(-) hosts which appear to have lost the capacity to suppress am mutations by ambiguity.

MeSH terms

  • Cell-Free System
  • Chromatography, DEAE-Cellulose
  • Coliphages / enzymology*
  • Coliphages / growth & development
  • Coliphages / metabolism
  • Crosses, Genetic
  • Cytosine Nucleotides
  • DNA Nucleotidyltransferases / biosynthesis*
  • DNA Nucleotidyltransferases / metabolism
  • DNA Replication
  • DNA Viruses / enzymology*
  • DNA Viruses / growth & development
  • DNA Viruses / metabolism
  • DNA, Viral / biosynthesis
  • Drug Resistance, Microbial
  • Escherichia coli / drug effects
  • Mutation*
  • Phosphoric Monoester Hydrolases / metabolism
  • Protein Biosynthesis*
  • Recombination, Genetic
  • Streptomycin / pharmacology
  • Suppression, Genetic*
  • Transferases / metabolism
  • Virus Replication


  • Cytosine Nucleotides
  • DNA, Viral
  • Transferases
  • DNA Nucleotidyltransferases
  • Phosphoric Monoester Hydrolases
  • Streptomycin