Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation
DC Field | Value | Language |
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dc.contributor.author | Warren D | - |
dc.contributor.author | Sam MD | - |
dc.contributor.author | Manley K | - |
dc.contributor.author | Sarkar D | - |
dc.contributor.author | Lee SY | - |
dc.contributor.author | Abbani M | - |
dc.contributor.author | Wojciak JM | - |
dc.contributor.author | Clubb RT | - |
dc.contributor.author | Landy A | - |
dc.date.accessioned | 2023-02-01T01:40:06Z | - |
dc.date.available | 2023-02-01T01:40:06Z | - |
dc.date.created | 2023-01-31 | - |
dc.date.issued | 2003-07 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/86808 | - |
dc.description.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 lint 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 amino-terminal 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. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.relation.isPartOf | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.title | Identification of the lambda integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000184222500027 | - |
dc.identifier.doi | 10.1073/pnas.1033041100 | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.100, no.14, pp.8176 - 8181 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.scopusid | 2-s2.0-0038154020 | - |
dc.citation.endPage | 8181 | - |
dc.citation.startPage | 8176 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 100 | - |
dc.citation.number | 14 | - |
dc.contributor.affiliatedAuthor | Lee SY | - |
dc.subject.keywordPlus | SITE-SPECIFIC RECOMBINATION | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | CATALYTIC DOMAIN | - |
dc.subject.keywordPlus | ATT-SITE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | DNA | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | EXCISIONASE | - |
dc.subject.keywordPlus | COOPERATIVITY | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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