@article{APS7567,
author = {Ling-Hua Meng and Xin-Xia He and Jin-Sheng Zhang and Jian Ding},
title = {DNA topoisomerase II as the primary cellular target for salvicine in Saccharomyces cerevisiae},
journal = {Acta Pharmacologica Sinica},
volume = {22},
number = {8},
year = {2016},
keywords = {},
abstract = {Aim: To identify whether DNA topoisomerase II (Topo II) is the primary cellular target of salvicine in Saccharomyces cerevisiae (S cerevisiae) and the action mode of salvicine.
Methods: The catalytic activity of Topo II was determined by Topo II mediated supercoiled pBR322 relaxation. The effects of salvicine on the growth of four strains of S cerevisiae were assessed by clone forming assay.
Results: Salvicine inhibited Topo II mediated supercoiled pBR322 relaxation in cell-free system. Cytotoxicities of salvicine to parent (JN394) and TOP1 deleted (JN394top1-) yeast cells were at the same level, suggesting Topo I might not be the cellular target of salvicine. Salvicine displayed high activity against JN394t2-1 cells at 25 degrees C, while no growth inhibition was observed at 30 degrees C in the concentration range of interest. Furthermore, JN394t2-5 cells which expressed top2-5 mutant allele were highly resistant to salvicine and etoposide (VP16).
Conclusion: Topo II was the primary cellular target of salvicine in vivo and salvicine killed yeast cells mainly by trapping the DNA-Topo II cleavage complex. Salvicine and VP16 might share some similar action locus on Topo II.},
issn = {1745-7254}, url = {http://www.chinaphar.com/article/view/7567}
}