NDLI: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation.

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Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Warren, David Landy, Arthur Sam, My D. Abbani, Mohamad Manley, Kate Wojciak, Jonathan M. Sarkar, Dibyendu Lee, Sang Yeol Clubb, Robert T.
Description	Author Affiliation: Warren D ( Division of Biology and Medicine, Brown University, Providence, RI 02912, USA.);
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 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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriophage Lambda Enzymology DNA Nucleotidyltransferases Chemistry Integrases Viral Proteins Binding Sites DNA Metabolism Dimerization Macromolecular Substances Models, Molecular Protein Binding Protein Conformation Protein Interaction Mapping Protein Structure, Tertiary Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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