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Revealing the mode of action of DNA topoisomerase I and its inhibitors by atomic force microscopy.

Abstract：

:In this study, we used, for the first time, atomic force microscope (AFM) images to investigate the mode of action of DNA topoisomerase I (topo I) in the presence and absence of its inhibitors: camptothecin (CPT) and tyrphostin AG-1387. The results revealed that in the absence of the inhibitors, the enzyme relaxed supercoiled DNA starting from a certain point in the DNA molecules and proceeded in one direction towards one of the edges of the DNA molecule. In addition, the relaxation of the supercoiled DNA is subsequently followed by a knotting event. In the presence of CPT, enzyme-supercoiled DNA complexes in which the enzyme is locked inside a relaxed region of the supercoiled DNA molecule were observed. Tyrphostin AG-1387 altered the DNA relaxation process of topo I producing unique shapes of DNA molecules. AFM images of the topo I protein provided a picture of the enzyme, which resembles its known crystallographic structure. Thus, AFM images provide new information on the mode of action of topo I in the absence and presence of its inhibitors.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Argaman M,Bendetz-Nezer S,Matlis S,Segal S,Priel E

doi

10.1016/s0006-291x(03)00025-1

subject

Has Abstract

pub_date

2003-02-14 00:00:00

pages

789-97

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X03000251

journal_volume

301

pub_type

杂志文章

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