Journal of Molecular Biology
Elements involved in site-specific recombination in bacteriophage lambda☆
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News from the protein mutability landscape
2013, Journal of Molecular BiologyCitation Excerpt :Comprehensive experimental mutagenesis studies confirmed that the effect of point mutations (SAAS) upon function depends crucially on their positions in the protein sequence [59–61]. Even within a unit as familiar as the DNA binding domain of the Escherichia coli LacI [62,63] repressor, almost any variant can be tolerated at some positions while, at others, all variants affect function (Fig. 2a). Simple structural constraints might suffice to explain this variability: to accommodate the negatively charged DNA, binding regions of the repressor contain positively charged residues.
Role for DNA homology in site-specific recombination. The isolation and characterization of a site affinity mutant of coliphage λ
1983, Journal of Molecular BiologySite-specific recombination. Xis-independent excisive recombination of bacteriophage lambda
1981, Journal of Molecular BiologyThe role of himA and xis in lambda site-specific recombination
1980, Journal of Molecular BiologyThe form of the DNA substrate required for excisive recombination of bacteriophage λ
1979, Journal of Molecular Biology
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One of us (S. G.) was a Fellow of the Jane Coffin Childs Memorial Fund for Medical Research while this work was done.
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Present address: Department of Biology, Massachusetts Institute of Technology, Cambridge, Mass. 02139, U.S.A.