Structural Activation of DNA Unwinding by MCM8/9/HROB
ATPase domains, reorganizing DNA-binding loops into a staircase configuration that supports DNA engagement. Remarkably, HROB associates with both halves of the heterohexamer and drives a similar rotation prior DNA binding for localizing MCM8/9 to sites of crosslink damage and unwinding, culminating in a unified mechanistic model for MCM8/9 helicase function and its activation by HROB.
Authors
- David R. McKinzey (ORCID: https://orcid.org/0000-0003-0845-5352)
- Chuxuan Li (ORCID: https://orcid.org/0000-0001-9386-9909)
- Michael A. Trakselis (ORCID: https://orcid.org/0000-0001-7054-8475)
- Temitope M Adeleke (ORCID: https://orcid.org/0009-0008-7041-6921)
- Yang Gao (ORCID: https://orcid.org/0000-0002-4037-0431)
- Colin To (ORCID: https://orcid.org/0009-0003-4462-1423)
Institutions
- Baylor University (US)
- Rice University (US)
Publication Details
- Journal
- bioRxiv (Cold Spring Harbor Laboratory)
- Published
- 2026-04-29
- DOI
- https://doi.org/10.64898/2026.04.28.721408
- Primary Topic
- DNA Repair Mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Science Foundation
- American Cancer Society