Mutations in the amino-terminal domain of lambda-integrase have differential effects on integrative and excisive recombination
DC Field | Value | Language |
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dc.contributor.author | Warren, D | - |
dc.contributor.author | Lee, SY | - |
dc.contributor.author | Landy, A | - |
dc.date.accessioned | 2023-02-07T14:40:05Z | - |
dc.date.available | 2023-02-07T14:40:05Z | - |
dc.date.created | 2023-02-07 | - |
dc.date.issued | 2005-02 | - |
dc.identifier.issn | 0950-382X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/86836 | - |
dc.description.abstract | Lambda integrase (Int) forms higher-order protein-DNA complexes necessary for site-specific recombination. The carboxy-terminal domain of Int (75-356) is responsible for catalysis at specific core-type binding sites whereas the amino-terminal domain (1-70) is responsible for cooperative arm-type DNA binding. Alanine scanning mutagenesis of residues 64-70, within full-length integrase, has revealed differential effects on cooperative arm binding interactions that are required for integrative and excisive recombination. Interestingly, while these residues are required for cooperative arm-type binding on both P'1,2 and P'2,3 substrates, cooperative binding at the arm-type sites P'2,3 was more severely compromised than binding at arm-type sites P'1,2 for L64A. Concomitantly, L64A had a much stronger effect on integrative than on excisive recombination. The arm-binding properties of Int appear to be intrinsic to the amino-terminal domain because the phenotype of L64A was the same in an amino-terminal fragment (Int 1-75) as it was in the full-length protein. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | WILEY | - |
dc.relation.isPartOf | MOLECULAR MICROBIOLOGY | - |
dc.title | Mutations in the amino-terminal domain of lambda-integrase have differential effects on integrative and excisive recombination | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000226707700012 | - |
dc.identifier.doi | 10.1111/j.1365-2958.2004.04447.x | - |
dc.identifier.bibliographicCitation | MOLECULAR MICROBIOLOGY, v.55, no.4, pp.1104 - 1112 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.scopusid | 2-s2.0-14544273672 | - |
dc.citation.endPage | 1112 | - |
dc.citation.startPage | 1104 | - |
dc.citation.title | MOLECULAR MICROBIOLOGY | - |
dc.citation.volume | 55 | - |
dc.citation.number | 4 | - |
dc.contributor.affiliatedAuthor | Lee, SY | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | SITE-SPECIFIC RECOMBINATION | - |
dc.subject.keywordPlus | PROTEIN-PROTEIN INTERACTIONS | - |
dc.subject.keywordPlus | BACTERIOPHAGE-LAMBDA | - |
dc.subject.keywordPlus | DNA-BINDING | - |
dc.subject.keywordPlus | SINGLE-BASE | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | ORDER | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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