Capp, Christopher and Qian, Yushen and Sage, Harvey and Huber, Harald and Hsieh, Tao-shih (2010) Separate and Combined Biochemical Activities of the Subunits of a Naturally Split Reverse Gyrase. JOURNAL OF BIOLOGICAL CHEMISTRY, 285 (51). pp. 39637-39645. ISSN 0021-9258, 1083-351X
Full text not available from this repository. (Request a copy)Abstract
Reverse gyrase reanneals denatured DNA and induces positive supercoils in DNA, an activity that is critical for life at very high temperatures. Positive supercoiling occurs by a poorly understood mechanism involving the coordination of a topoisomerase domain and a helicase-like domain. In the parasitic archaeon Nanoarchaeum equitans, these domains occur as separate subunits. We express the subunits, and characterize them both in isolation and as a heterodimer. Each subunit tightly associates and interacts with the other. The topoisomerase subunit enhances the catalytic specificity of the DNA-dependent ATPase activity of the helicase-like subunit, and the helicase-like subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling. DNA binding preference for both single-and double-stranded DNA is partitioned between the subunits. Based on a sensitive topological shift assay, the binding preference of helicase-like subunit for underwound DNA is modulated by its binding with ATP cofactor. These results provide new insight into the mechanism of positive supercoil induction by reverse gyrase.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HELICASE-LIKE DOMAIN; NANOARCHAEUM-EQUITANS; DNA; TOPOISOMERASE; HYPERTHERMOPHILES; INSIGHTS; ASSOCIATION; EVOLUTION; TOPOLOGY; MACHINE; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 06 Jul 2020 07:16 |
| Last Modified: | 06 Jul 2020 07:16 |
| URI: | https://pred.uni-regensburg.de/id/eprint/23733 |
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