Characterization of amber mutations in bacteriophage Mu transposase: a functional analysis of the protein.
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.
Desmet
L
L
Département de Biologie Moléculaire, Université Libre de Bruxelles, Rhode-St-Genèse, Belgium.
Faelen
M
M
Gama
M J
MJ
Ferhat
A
A
Toussaint
A
A
D000595:Amino Acid Sequence; D010583:Bacteriophage mu / Q000201:enzymology* / Q000254:growth & development / Q000502:physiology; D001483:Base Sequence; D015153:Blotting, Western; D004251:DNA Transposable Elements; D007106:Immune Sera; D008242:Lysogeny; D008969:Molecular Sequence Data; D009154:Mutation; D009713:Nucleotidyltransferases / Q000235:genetics / Q000502:physiology*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000502:physiology; D013489:Suppression, Genetic; D019895:Transposases
D004251:DNA Transposable Elements; D007106:Immune Sera; D011994:Recombinant Proteins; D009713:Nucleotidyltransferases; D019895:Transposases