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Conservation of Structure and Mechanism between Eukaryotic Topoisomerase I and Site-Specific Recombinases

Published in: Cell

Date of publication: March 20, 1998

Language: English

Bibliographic databases:

Cites articles 40

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Step-arrest mutants of FLP recombinase: implications for the catalytic mechanism of DNA recombination
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Peptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I.
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Vaccinia DNA topoisomerase I promotes illegitimate recombination in Escherichia coli
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DNA specificity of the Cre recombinase resides in the 25 kDa carboxyl domain of the protein
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Phenotypic selection and characterization of mutant alleles of a eukaryotic DNA topoisomerase I.
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Improved methods for building protein models in electron density maps and the location of errors in these models
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Eukaryotic topoisomerase I-DNA interaction is stabilized by helix curvature
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Recombination mediated by vaccinia virus DNA topoisomerase I in Escherichia coli is sequence specific
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Protein structure comparison by alignment of distance matrices
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Appendix. II: Alignment of primary sequences of DNA topoisomerases
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Crystal structure of the amino-terminal fragment of vaccinia virus DNA topoisomerase I at 1.6 A resolution
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Resolution of Holliday junctions by eukaryotic DNA topoisomerase I

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Mutational analysis of 39 residues of vaccinia DNA topoisomerase identifies Lys-220, Arg-223, and Asn-228 as important for covalent catalysis
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