Mutations in the carboxy-terminal part of IS30 transposase affect the formation and dissolution of (IS30)2 dimer.
FEBS Lett
; 413(3): 453-61, 1997 Aug 25.
Article
em En
| MEDLINE
| ID: mdl-9303555
ABSTRACT
The transposase of IS30 catalyses different transpositional rearrangements via the dimer (IS30)2 intermediate structure. Mutation analysis provides evidence that the C-terminal part of IS30 transposase is required for the formation and dissolution of (IS30)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 (IS30)2 intermediate structure. The transposase part studied shows significant homologies in three highly conserved regions to proteins of IS30-related mobile elements.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
DNA Nucleotidiltransferases
Idioma:
En
Ano de publicação:
1997
Tipo de documento:
Article