Buckley, Ryan J. and Kramm, Kevin and Cooper, Christopher D. O. and Grohmann, Dina and Bolt, Edward L. (2020) Mechanistic insights into Lhr helicase function in DNA repair. BIOCHEMICAL JOURNAL, 477 (16). pp. 2935-2947. ISSN 0264-6021, 1470-8728
Full text not available from this repository. (Request a copy)Abstract
The DNA helicase Large helicase-related (Lhr) is present throughout archaea, including in the Asgard and Nanoarchaea, and has homologues in bacteria and eukaryotes. It is thought to function in DNA repair but in a context that is not known. Our data show that archaeal Lhr preferentially targets DNA replication fork structures. In a genetic assay, expression of archaeal Lhr gave a phenotype identical to the replication-coupled DNA repair enzymes Hel308 and RecQ. Purified archaeal Lhr preferentially unwound model forked DNA substrates compared with DNA duplexes, flaps and Holliday junctions, and unwound them with directionality. Single-molecule FRET measurements showed that binding of Lhr to a DNA fork causes ATP-independent distortion and base-pair melting at, or close to, the fork branchpoint. ATP-dependent directional translocation of Lhr resulted in fork DNA unwinding through the `parental' DNA strands. Interaction of Lhr with replication forks in vivo and in vitro suggests that it contributes to DNA repair at stalled or broken DNA replication.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SINGLE-MOLECULE; PROTEIN; BINDING; IDENTIFICATION; GENE; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Dina Grohmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 17 Mar 2021 12:49 |
| Last Modified: | 17 Mar 2021 12:49 |
| URI: | https://pred.uni-regensburg.de/id/eprint/44069 |
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