Intradimerically tethered DNA topoisomerase II is catalytically active in DNA transport.
收藏PubMed Central1996-04-02 更新2026-05-02 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC39745/
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资源简介：
A covalently cross-linked dimer of yeast DNA topoisomerase II was created by fusing the enzyme with the GCN4 leucine zipper followed by two glycines and a cysteine. Upon oxidation of the chimeric protein, a disulfide bond forms between the two carboxyl termini, covalently and intradimerically cross-linking the two protomers. In addition, all nine of the cysteines naturally occurring in topoisomerase II have been changed to alanines in this construct. This cross-linked, cysteine-less topoisomerase II is catalytically active in DNA duplex passage as indicated by ATP-dependent DNA supercoil relaxation and kinetoplast DNA decatenation assays. However, these experiments do not directly distinguish between a "one-gate" and a "two-gate" mechanism for the enzyme. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1996-04-02
