F. Olasz et al., MUTATIONS IN THE CARBOXY-TERMINAL PART OF IS30 TRANSPOSASE AFFECT THEFORMATION AND DISSOLUTION OF (IS30)(2) DIMER, FEBS letters, 413(3), 1997, pp. 453-461
The transposase of IS30 catalyses different transpositional rearrangem
ents via the dimer (IS30)(2) intermediate structure. Mutation analysis
provides evidence that the C-terminal part of IS30 transposase is req
uired for the formation and dissolution of (IS30)(2) dimer. C-terminal
mutants are also defective in transpositional fusion; however, this d
eficiency can be 'suppressed' by addition of the final product of site
-specific dimerisation, the core (IS30)(2) intermediate structure. The
transposase part studied shows significant homologies in three highly
conserved regions to proteins of IS30-related mobile elements. (C) 19
97 Federation of European Biochemical Societies.