Instability of bacteriophage Mu transposase and the role of host Hfl protein.
The activity of the transposase of bacteriophage Mu is unstable, requiring the protein to be synthesized throughout the lytic cycle (Pato and Reich, 1982). Using Western blot analysis, we analysed the stability of the transposase protein during the lytic cycle and found that it, too, is unstable. The instability of the protein is observed both in the presence and the absence of Mu DNA replication, and is independent of other Mu-encoded proteins and the transposase binding sites at the Mu genome ends. Stability of the protein is enhanced in host strains mutated at the hfl locus; however, stability of the transposase activity is not enhanced in these strains, suggesting that functional inactivation of the protein is not simply a result of its proteolysis.
Gama
M J
MJ
Unité Transposition Bactérienne et Bactéries Phytopathogènes, Université Libre de Bruxelles, Rhode StGenèse, Belgium.
Toussaint
A
A
Pato
M L
ML
D010583:Bacteriophage mu / Q000201:enzymology* / Q000235:genetics; D004261:DNA Replication; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005814:Genes, Viral; D009154:Mutation; D009713:Nucleotidyltransferases / Q000378:metabolism*; D010957:Plasmids; D019895:Transposases; D014764:Viral Proteins / Q000378:metabolism*
D014764:Viral Proteins; D009713:Nucleotidyltransferases; D019895:Transposases