Initiation of phage phi 29 DNA replication by the terminal protein modified at the carboxyl end

Nucleic Acids Res. 1983 Nov 11;11(21):7397-407. doi: 10.1093/nar/11.21.7397.

Abstract

A mutant at the carboxyl end of the terminal protein, p3, of phage phi 29 DNA has been constructed by inserting an containing the stop translation codon TGA in the three possible reading frames, immediately downstream of a phage phi 29 DNA fragment coding for all but the last five amino acids of protein p3. The activity in the formation of the p3-dAMP initiation complex in vitro of this mutant as well as another one previously isolated, also mutated at the carboxyl end, have been tested. The results obtained suggest that an intact carboxyl end in the phage phi 29 terminal protein is essential for its normal primer function in DNA replication.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacillus subtilis / genetics*
  • Bacteriophages / genetics*
  • Codon
  • DNA Replication*
  • DNA Restriction Enzymes
  • DNA, Recombinant / metabolism
  • Deoxyadenine Nucleotides / metabolism
  • Kinetics
  • Mutation
  • Plasmids
  • Protein Biosynthesis
  • Viral Proteins / genetics*
  • Viral Proteins / isolation & purification

Substances

  • Codon
  • DNA, Recombinant
  • Deoxyadenine Nucleotides
  • Viral Proteins
  • 2'-deoxy-5'-adenosine monophosphate
  • DNA Restriction Enzymes