期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:1981
卷号:78
期号:2
页码:843-847
DOI:10.1073/pnas.78.2.843
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:Escherichia coli omega protein, a type 1 topoisomerase, can catenate and knot duplex DNA circles. Previously, these activities were thought to be limited to type 2 topoisomerases. Catenation by omega requires a nick in one of the participating molecules, but it is not necessary that both be nicked. Catenation does not depend on sequence homology and is greatly stimulated by DNA-condensing agents such as spermidine. A eukaryotic type 1 topoisomerase can also interlock duplex DNA circles. These activities cannot easily be explained by the widely held topoisomerase model in which a reversible nick in DNA allows free rotation about the unbroken strand. We suggest instead passage of a DNA segment though a transient enzyme-bridged break in a single DNA strand. This is analogous to the sign inversion mechanism of the type 2 topoisomerases, and thus expresses an essential mechanistic unity among topoisomerases. As expected for relaxation by a single-strand passage, omega changes the linking number of DNA in steps of 1.