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J. Biol. Chem., Vol. 263, Issue 31, 15857-15859, Nov, 1988
YC Tse-Dinh and RK Beran-Steed
Escherichia coli DNA topoisomerase I catalyzes interconversions of
different DNA topological isomers by the breakage and rejoining of DNA
phosphodiester bonds. It has a crucial role in maintaining an optimal DNA
superhelicity in E. coli. It is a single polypeptide of 864 amino acids.
Analysis of the amino acid sequence reveals three tandem repeat units each
containing two pairs of cysteines suggesting that each unit may form a
zinc-binding domain. We have determined that each enzyme molecule contains
three to four zinc atoms using inductively coupled plasma-atomic emission
analysis. Modification of the cysteine residues and removal of the zinc
from the enzyme result in loss of activity. Zinc ions are needed for full
recovery of enzyme activity when the cysteine modification is reversed.
Comparison with the zinc-binding domains of the sequence-specific
DNA-binding proteins shows significant differences.
Escherichia coli DNA topoisomerase I is a zinc metalloprotein with three repetitive zinc-binding domains
Central Research and Development, E. I. du Pont de Nemours & Co., Wilmington, Delaware 19898.
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