Phage Mu transposase: deletion of the carboxy-terminal end does not abolish DNA-binding activity.
We demonstrate that a specific site on the transposase protein, pA, of bacteriophage Mu is highly susceptible to proteolytic cleavage. Cleavage is observed in a minicell system on solubilisation with the non-ionic detergent Triton X-100 or following addition of a solubilised minicell preparation to pA synthesised in a cell-free coupled transcription/translation system. Cleavage occurs at the carboxy-terminal end of the protein and generates a truncated polypeptide of 64 kDa, pA*, which retains some of the DNA-binding properties of pA. These results suggest that pA may be divided into functional domains for DNA binding and for interaction with the proteins involved in phage replication.
Betermier
M
M
C.R.B.G.C. du C.N.R.S., Toulouse, France.
Alazard
R
R
Ragueh
F
F
Roulet
E
E
Toussaint
A
A
Chandler
M
M
D010583:Bacteriophage mu / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D001665:Binding Sites; D004279:DNA, Viral / Q000378:metabolism*; D009713:Nucleotidyltransferases / Q000235:genetics / Q000378:metabolism*; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism; D010957:Plasmids; D011499:Protein Processing, Post-Translational; D019895:Transposases; D014779:Virus Replication
D004279:DNA, Viral; D010446:Peptide Fragments; D009713:Nucleotidyltransferases; D019895:Transposases