Function of the hydrophilic carboxyl terminus of type II DNA topoisomerase from Drosophila melanogaster. II. In vivo studies.

@article{Crenshaw1993FunctionOT,
  title={Function of the hydrophilic carboxyl terminus of type II DNA topoisomerase from Drosophila melanogaster. II. In vivo studies.},
  author={D G Crenshaw and Tao Shih Hsieh},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 28},
  pages={21335-43}
}
Genetic complementation, protein distribution, and in vivo enzymatic activity by carboxyl-terminal truncation mutations of the Drosophila enzyme were examined. Removal of more than 273 of the 1447 amino acids composing the full-length topoisomerase inactivates the enzyme in vivo and in vitro; removal of 227 amino acids or less has no apparent effect on the ability of the enzyme to substitute for a conditional lethal, or null mutation, of the Saccharomyces cerevisiae top2 gene. Four… CONTINUE READING