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• W2019917384 abstract "Lambda integrase (Int) is a heterobivalent DNA-binding protein that together with the accessory DNA-bending proteins IHF, Fis, and Xis, forms the higher-order protein–DNA complexes that execute integrative and excisive recombination at specific loci on the chromosomes of phage λ and its Escherichia coli host. The large carboxyl-terminal domain of Int is responsible for binding to core-type DNA sites and catalysis of DNA cleavage and ligation reactions. The small amino-terminal domain (residues 1–70), which specifies binding to arm-type DNA sites distant from the regions of strand exchange, consists of a three-stranded β-sheet, proposed to recognize the cognate DNA site, and an α-helix. We report here that a site on this α-helix is critical for both homomeric interactions between Int protomers and heteromeric interactions with Xis. The mutant E47A, which was identified by alanine-scanning mutagenesis, abolishes interactions between Int and Xis bound at adjacent binding sites and reduces interactions between Int protomers bound at adjacent arm-type sites. Concomitantly, this residue is essential for excisive recombination and contributes to the efficiency of the integrative reaction. NMR titration data with a peptide corresponding to Xis residues 57–69 strongly suggest that the carboxyl-terminal tail of Xis and the α-helix of the aminoterminal domain of Int comprise the primary interaction surface for these two proteins. The use of a common site on λ Int for both homotypic and heterotypic interactions fits well with the complex regulatory patterns associated with this site-specific recombination reaction." @default.
• W2019917384 created "2016-06-24" @default.
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• W2019917384 date "2003-06-27" @default.
• W2019917384 modified "2023-10-16" @default.
• W2019917384 title "Identification of the λ integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation" @default.
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• W2019917384 doi "https://doi.org/10.1073/pnas.1033041100" @default.
• W2019917384 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/166202" @default.
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