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Mutations in the carboxy‐terminal part of IS 30 transposase affect the formation and dissolution of (IS 30 ) 2 dimer
Author(s) -
Olasz Ferenc,
Farkas Tibor,
Stalder Rolf,
Arber Werner
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00947-2
Subject(s) - transposase , dimer , transposable element , mutant , mutation , chemistry , stereochemistry , gene , biochemistry , organic chemistry
The transposase of IS 30 catalyses different transpositional rearrangements via the dimer (IS 30 ) 2 intermediate structure. Mutation analysis provides evidence that the C‐terminal part of IS 30 transposase is required for the formation and dissolution of (IS 30 ) 2 dimer. C‐terminal mutants are also defective in transpositional fusion; however, this deficiency can be `suppressed' by addition of the final product of site‐specific dimerisation, the core (IS 30 ) 2 intermediate structure. The transposase part studied shows significant homologies in three highly conserved regions to proteins of IS 30 ‐related mobile elements.