Characterisation of an IS1 induced mutation in the carboxy-terminal end of bacteriophage Mu transposase which affects several functional domains of the protein.

Abstract excerpt

We show that a mutation in bacteriophage Mu transposase (pA) which was isolated as a deletion of the C-terminal end of the protein actually consists of the replacement of the last 16 amino acids (which are mostly hydrophilic) by 26 mostly hydrophobic amino acids. This change almost completely inactivates the in vivo enzyme activity as well as its capacity to bind Mu ends in vitro, although the end-binding domain...

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