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

Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation.
type: AcademicArticle
type: Article
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.
date: 2003-07-08
volume: 100
issue: 14
is part of: Proceedings of the National Academy of Sciences of the United States of America
status: peerReviewed
status: published
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository
has document: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
has version: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
has published: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
has document: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (Indexer Terms)
has document: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (Image (PNG))
subject: Q Science (General)

Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
type: Document
has file: sarkar2003.pdf
has part: sarkar2003.pdf

National Academy of Sciences
type: Organization

Proceedings of the National Academy of Sciences of the United States of America
type: Collection
issn: 00278424

Jonathan M Wojciak
type: Person
given name: Jonathan M
family name: Wojciak

Mohamad Abbani
type: Person
given name: Mohamad
family name: Abbani

Sang Yeol Lee
type: Person
given name: Sang Yeol
family name: Lee

Dibyendu Sarkar
type: Person
given name: Dibyendu
family name: Sarkar

Kate Manley
type: Person
given name: Kate
family name: Manley

Robert T Clubb
type: Person
given name: Robert T
family name: Clubb

My D Sam
type: Person
given name: My D
family name: Sam

David Warren
type: Person
given name: David
family name: Warren

Arthur Landy
type: Person
given name: Arthur
family name: Landy

Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (Indexer Terms)
type: Document
is version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
is volatile version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
is index codes version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
has file: indexcodes.txt
has part: 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))
type: Document
is version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
is volatile version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
islightbox thumbnail version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
has file: lightbox.jpg
has part: 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))
type: Document
is version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
is volatile version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
ispreview thumbnail version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
has file: preview.jpg
has part: 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))
type: Document
is version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
is volatile version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
ismedium thumbnail version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
has file: medium.jpg
has part: 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))
type: Document
is version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
is volatile version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
issmall thumbnail version of: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation. (PDF)
has file: small.jpg
has part: small.jpg

HTML Summary of #929 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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primary topic: Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation.

Q Science (General)
type: Concept