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Structural features of Dnase1L3 responsible for serum antigen clearance
Open accessPreprint — published as 10.1038/s42003-022-03755-5 · Paper page
Abstract
Autoimmunity develops when extracellular DNA released from dying cells is not cleared from serum. While serum DNA is primarily digested by Dnase1 and Dnase1L3, Dnase1 does not rescue autoimmunity arising from Dnase1L3 deficiencies. Dnase1L3 uniquely degrades antigenic forms of cell-free DNA, including DNA complexed with lipids and proteins. The distinct activity of Dnase1L3 relies on its unique C-terminal Domain (CTD), but the mechanism is unknown. We used multiple biophysical techniques and functional assays to study the interplay between the core catalytic domain and the CTD. While the core domain resembles Dnase1, there are several key differences between the two enzymes. Dnase1L3 is not inhibited by actin due to multiple differences in the actin recognition site. The CTD augments the ability of the core to bind DNA, thereby facilitating the degradation of complexed DNA to prevent autoimmune pathology. Together, these structural insights will inform the development of Dnase1L3-based therapies for autoimmunity.
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Metadata
- Authors
- McCord, J. J., Engavale, M., Masoumzadeh, E., Villarreal, J., Mapp, B., Latham, M. P., Keyel, P. A., & Sutton, R. B.
- Affiliations
- Texas Tech University (US)
- Corresponding author
- Sutton, R. Bryan
- ORCID
- Venue
- Communications Biology
- Publisher
- openRxiv
- Published
- 2022-01-20
- Volume
- 5
- Issue
- 1
- Pages
- 825-825
- ISSN
- 2399-3642 (ISSN-L)
- PMC
- PMC9381713
- OpenAlex
- W4292004599
- Cited by
- 31
- References
- 1
- Citations by year
- 2026: 10 · 2025: 8 · 2024: 6 · 2023: 6 · 2022: 1
- FWCI
- 3.81
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Communications Biology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- ThinkTech (Texas Tech University) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- U.S. Department of Energy (76SF00515, DE–AC02–76SF00515, AC02‐76SF00515, No. DE-AC02–76SF00515, Contract No. DE-AC02-76SF00515, P30-GM133894, DE-AC02-)
- CH Foundation
- Texas Tech University
- Lupus Research Alliance (707050)
- Texas Tech University Health Sciences Center
- National Institutes of Health (DE-AC02-76SF00515)
- Office of Science (AC02-76SF00515, DE-AC02-76SF0051 5, DE-AC02, P30GM133894, 76SF00515)
- National Institute of General Medical Sciences (DE-AC02-76SF00515, P30GM133894, R35GM128906)
- Basic Energy Sciences (DE-AC02, P30GM133894, 76SF00515, Contract No. DE-AC02-76SF00515, AC02-76SF00515, DE-AC-02-76SF00515)
- Biological and Environmental Research (DE- AC0276SF00515, P30GM133894)
- SLAC National Accelerator Laboratory (DEAC02−76SF00515, AC02‐76SF00515, Contract No. DE-AC02-76SF00515)
- Topics
- Health Sciences › Medicine › Rheumatology › Systemic Lupus Erythematosus Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- DNASE1L3, DNase1, autoimmunity, cell-free DNA, C-terminal domain, DNA binding, DNA degradation, autoimmune disease therapy
- MeSH terms
- Actins, DNA, Endodeoxyribonucleases
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