<> "The repository administrator has not yet configured an RDF license."^^ . <> . . . "Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation."^^ . "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 lambda 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 beta-sheet, proposed to recognize the cognate DNA site, and an alpha-helix. We report here that a site on this alpha-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 alpha-helix of the aminoterminal domain of Int comprise the primary interaction surface for these two proteins. The use of a common site on lambda Int for both homotypic and heterotypic interactions fits well with the complex regulatory patterns associated with this site-specific recombination reaction."^^ . "2003-07-08" . . "100" . "14" . . "National Academy of Sciences"^^ . . . "Proceedings of the National Academy of Sciences of the United States of America"^^ . . . "00278424" . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . "Jonathan M"^^ . "Wojciak"^^ . "Jonathan M Wojciak"^^ . . "Mohamad"^^ . "Abbani"^^ . "Mohamad Abbani"^^ . . "Sang Yeol"^^ . "Lee"^^ . "Sang Yeol Lee"^^ . . "Dibyendu"^^ . "Sarkar"^^ . "Dibyendu Sarkar"^^ . . "Kate"^^ . "Manley"^^ . "Kate Manley"^^ . . "Robert T"^^ . "Clubb"^^ . "Robert T Clubb"^^ . . "My D"^^ . "Sam"^^ . "My D Sam"^^ . . "David"^^ . "Warren"^^ . "David Warren"^^ . . "Arthur"^^ . "Landy"^^ . "Arthur Landy"^^ . . . . . . "Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)"^^ . . . . . "sarkar2003.pdf"^^ . . . "Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (Indexer Terms)"^^ . . . . . . "indexcodes.txt"^^ . . . "Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (Image (PNG))"^^ . . . . . . "lightbox.jpg"^^ . . . "Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (Image (PNG))"^^ . . . . . . "preview.jpg"^^ . . . "Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (Image (PNG))"^^ . . . . . . "medium.jpg"^^ . . . "Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (Image (PNG))"^^ . . . . . . "small.jpg"^^ . . "HTML Summary of #929 \n\nIdentification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation.\n\n" . "text/html" . . . "Q Science (General)"@en . .