Mutations in the amino-terminal domain of lambda-integrase have differential effects on integrative and excisive recombinationopen access
- Authors
- Warren, D; Lee, SY; Landy, A
- Issue Date
- Feb-2005
- Publisher
- WILEY
- Citation
- MOLECULAR MICROBIOLOGY, v.55, no.4, pp.1104 - 1112
- Journal Title
- MOLECULAR MICROBIOLOGY
- Volume
- 55
- Number
- 4
- Start Page
- 1104
- End Page
- 1112
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/86836
- DOI
- 10.1111/j.1365-2958.2004.04447.x
- ISSN
- 0950-382X
- 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.
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