Mutations in the carboxy-terminal part of IS30 transposase affect the formation and dissolution of (IS30)2 dimer

F. Olasz, Tibor Farkas, Rolf Stalder, Werner Arber

Research output: Contribution to journalArticle

9 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)453-461
Number of pages9
JournalFEBS Letters
Volume413
Issue number3
DOIs
Publication statusPublished - Aug 25 1997

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Transposases
Dimers
Dissolution
Mutation
Dimerization
Fusion reactions
Proteins

Keywords

  • Domain structure of transposase
  • Escherichia coli
  • Insertion sequence
  • Intermediate in transposition
  • IS30
  • Site-specific deletion formation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Mutations in the carboxy-terminal part of IS30 transposase affect the formation and dissolution of (IS30)2 dimer. / Olasz, F.; Farkas, Tibor; Stalder, Rolf; Arber, Werner.

In: FEBS Letters, Vol. 413, No. 3, 25.08.1997, p. 453-461.

Research output: Contribution to journalArticle

Olasz, F. ; Farkas, Tibor ; Stalder, Rolf ; Arber, Werner. / Mutations in the carboxy-terminal part of IS30 transposase affect the formation and dissolution of (IS30)2 dimer. In: FEBS Letters. 1997 ; Vol. 413, No. 3. pp. 453-461.
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