Summary
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.
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Betermier, M., Alazard, R., Ragueh, F. et al. Phage Mu transposase: deletion of the carboxy-terminal end does not abolish DNA-binding activity. Mol Gen Genet 210, 77–85 (1987). https://doi.org/10.1007/BF00337761
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DOI: https://doi.org/10.1007/BF00337761