Characterization of amber mutations in bacteriophage Mu transposase: a functional analysis of the protein

Mol Microbiol. 1989 Sep;3(9):1145-58. doi: 10.1111/j.1365-2958.1989.tb00265.x.

Abstract

We have characterized a series of amber mutations in the A gene of bacteriophage Mu encoding the phage transposase. We tested different activities of these mutant proteins either in a sup0 strain or in different sup bacteria. In conjunction with the results described in the accompanying paper by Bétermier et al. (1989) we find that the C-terminus of the protein is not absolutely essential for global transposase function, but is essential for phage growth. Specific binding to Mu ends is defined by a more central domain. Our results also reinforce the previous findings (Bétermier et al., 1987) that more than one protein may be specified by the A gene.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage mu / enzymology*
  • Bacteriophage mu / growth & development
  • Bacteriophage mu / physiology
  • Base Sequence
  • Blotting, Western
  • DNA Transposable Elements
  • Immune Sera
  • Lysogeny
  • Molecular Sequence Data
  • Mutation
  • Nucleotidyltransferases / genetics
  • Nucleotidyltransferases / physiology*
  • Protein Binding
  • Recombinant Proteins / physiology
  • Suppression, Genetic
  • Transposases

Substances

  • DNA Transposable Elements
  • Immune Sera
  • Recombinant Proteins
  • Nucleotidyltransferases
  • Transposases

Associated data

  • GENBANK/UNKNOWN