Esha Dalvie
B.S. Molecular Toxicology, University of California, Berkeley
Ph.D. , Biochemistry, Vanderbilt University
Postdoctoral Fellow, MIT
Type II topoisomerases interact differently with different substrates of DNA supercoil handedness, which can influence where the enzyme acts during DNA processes. When relaxing DNA supercoils, human topoisomerase IIα and bacterial topoisomerase IV have been shown to recognize DNA supercoil handedness, while human topoisomerase IIβ shows no preference. Another function of these enzymes is the decatenation of DNA prior to mitosis. Cellular studies in yeast and bacteria have suggested that DNA in vivo becomes positively supercoiled through interaction with condensins prior to decatenation. My project focuses on whether type II topoisomerases possess an intrinsic ability to recognize DNA supercoil handedness during catenation and decatenation.