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

Ferenc 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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Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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