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TitleCoordinated DNA polymerization by Polγ and the region of LonP1 regulated proteolysis.
Journal, issue, pagesNucleic Acids Res, Vol. 52, Issue 13, Page 7863-7875, Year 2024
Publish dateJul 22, 2024
AuthorsAmanda A Riccio / Asia J Brannon / Juno M Krahn / Jonathan Bouvette / Jason G Williams / Mario J Borgnia / William C Copeland /
PubMed AbstractThe replicative mitochondrial DNA polymerase, Polγ, and its protein regulation are essential for the integrity of the mitochondrial genome. The intricacies of Polγ regulation and its interactions ...The replicative mitochondrial DNA polymerase, Polγ, and its protein regulation are essential for the integrity of the mitochondrial genome. The intricacies of Polγ regulation and its interactions with regulatory proteins, which are essential for fine-tuning polymerase function, remain poorly understood. Misregulation of the Polγ heterotrimer, consisting of (i) PolG, the polymerase catalytic subunit and (ii) PolG2, the accessory subunit, ultimately results in mitochondrial diseases. Here, we used single particle cryo-electron microscopy to resolve the structure of PolG in its apoprotein state and we captured Polγ at three intermediates within the catalytic cycle: DNA bound, engaged, and an active polymerization state. Chemical crosslinking mass spectrometry, and site-directed mutagenesis uncovered the region of LonP1 engagement of PolG, which promoted proteolysis and regulation of PolG protein levels. PolG2 clinical variants, which disrupted a stable Polγ complex, led to enhanced LonP1-mediated PolG degradation. Overall, this insight into Polγ aids in an understanding of mitochondrial DNA replication and characterizes how machinery of the replication fork may be targeted for proteolytic degradation when improperly functioning.
External linksNucleic Acids Res / PubMed:38932681 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 4.2 Å
Structure data

42979

8v54

EMDB-42979, PDB-8v54:
Engaged conformation of the human mitochondrial DNA polymerase gamma bound to DNA
Method: EM (single particle) / Resolution: 4.1 Å

42980

8v55

EMDB-42980, PDB-8v55:
Human mitochondrial DNA polymerase gamma bound to a replication fork in an open conformation
Method: EM (single particle) / Resolution: 4.2 Å

42982

8v5d

EMDB-42982, PDB-8v5d:
Human mitochondrial DNA polymerase catalytic subunit, PolG, in an APO conformation
Method: EM (single particle) / Resolution: 3.0 Å

42984

8v5r

EMDB-42984, PDB-8v5r:
Active conformation of DNA polymerase gamma bound to DNA
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-D3T:
2',3'-DIDEOXY-THYMIDINE-5'-TRIPHOSPHATE

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN/DNA / Mitochondria DNA polymerase / DNA polymerase gamma / Mitochondrial DNA replication / DNA binding protein / DNA BINDING PROTEIN-DNA complex / DNA polymerase / DNA polymerase catalytic subunit

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