Abstract 1614 Investigating the Role of DNA Binding in the Allosteric Regulation of LONP1 Protease
Human mitochondrial LONP1 is an ATP-dependent enzyme that is a therapeutic target in acute myeloid leukemia (AML). LONP1 is a multifunctional protein complex with protease function to degrade damaged proteins, chaperone function to rescue misfolded proteins, and a weakly characterized DNA-binding function to regulate mitochondrial genome maintenance and expression. LONP1 activity is governed by allosteric regulation. For instance, ATP binding to the ATPase domain significantly enhances the activity of the distal protease domain.
Authors
- Matthew Tcheng (ORCID: https://orcid.org/0000-0001-5440-6434)
- Mohammad T. Mazhab‐Jafari (ORCID: https://orcid.org/0000-0003-0207-5877)
- Aaron David Schimmer (ORCID: https://orcid.org/0000-0003-4023-3899)
- Siavash Vahidi (ORCID: https://orcid.org/0000-0001-8637-3710)
- Alexander Keszei
- Stefan Currie (ORCID: https://orcid.org/0009-0000-9652-6901)
- Rachel Wideman
Institutions
- University of Wisconsin–La Crosse (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109908
- Primary Topic
- ATP Synthase and ATPases Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Institutes of Health
- Canadian Institutes of Health Research
- National Institute of General Medical Sciences