Activity of coliphage HK022 excisionase (Xis) in the absence of DNA binding

Pnina Gottfried, Nava Silberstein, Ezra Yagil, Mikhail Kolot*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


A mutated excisionase (Xis) protein of coliphage HK022 whose single Cys residue was replaced by Ser does not bind to its two tandem binding sites (X1, X2) on the P arm of attR. Despite its DNA-binding inability the protein showed 30% excision activity of the wild type Xis both in vitro and in vivo. This partial activity is attributed to the interaction of Xis with integrase that is retained in the mutant protein. This protein-protein interaction occurs in the absence of DNA binding.

Original languageEnglish
Pages (from-to)133-138
Number of pages6
JournalFEBS Letters
Issue number2-3
StatePublished - 19 Jun 2003


FundersFunder number
Israel Academy of Sciences and Humanities637/02
Israel Science Foundation


    • Bacteriophage HK022
    • DNA-protein interaction
    • Excisionase
    • Fluorescence resonance energy transfer
    • Protein-protein interaction
    • Site-specific recombination


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