PMID:1317847
| Citation |
Oram, M and Fisher, LM (1992) An Escherichia coli DNA topoisomerase I mutant has a compensatory mutation that alters two residues between functional domains of the DNA gyrase A protein. J. Bacteriol. 174:4175-8 |
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| Abstract |
Nucleotide sequence analysis revealed that the compensatory gyrA mutation in Escherichia coli DM750 affects DNA supercoiling by interchanging the identities of Ala-569 and Thr-586 in the DNA gyrase A subunit. These residues flank Arg-571, a site for trypsin cleavage that splits gyrase A protein between DNA breakage-reunion and DNA-binding domains. The putative interdomain locations of the DM750 mutation and that of E. coli DM800 (in gyrase B protein) suggests that these compensatory mutations may reduce DNA supercoiling activity by altering allosteric interactions in the gyrase complex. |
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| Keywords |
Amino Acid Sequence; Base Sequence; DNA Topoisomerases, Type I/chemistry; DNA Topoisomerases, Type I/genetics; DNA Topoisomerases, Type II/chemistry; DNA Topoisomerases, Type II/genetics; DNA Topoisomerases, Type II/metabolism; DNA, Superhelical/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Molecular Sequence Data; Mutation/genetics; Oligodeoxyribonucleotides/genetics; Polymerase Chain Reaction; Restriction Mapping |
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