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TitleAutophosphorylation transforms DNA-PK from protecting to processing DNA ends.
Journal, issue, pagesMol Cell, Vol. 82, Issue 1, Page 177-189.e4, Year 2022
Publish dateJan 6, 2022
AuthorsLan Liu / Xuemin Chen / Jun Li / Huaibin Wang / Christopher J Buehl / Noah J Goff / Katheryn Meek / Wei Yang / Martin Gellert /
PubMed AbstractThe DNA-dependent protein kinase (DNA-PK) initially protects broken DNA ends but then promotes their processing during non-homologous end joining (NHEJ). Before ligation by NHEJ, DNA hairpin ends ...The DNA-dependent protein kinase (DNA-PK) initially protects broken DNA ends but then promotes their processing during non-homologous end joining (NHEJ). Before ligation by NHEJ, DNA hairpin ends generated during V(D)J recombination must be opened by the Artemis nuclease, together with autophosphorylated DNA-PK. Structures of DNA-PK bound to DNA before and after phosphorylation, and in complex with Artemis and a DNA hairpin, reveal an essential functional switch. When bound to open DNA ends in its protection mode, DNA-PK is inhibited for cis-autophosphorylation of the so-called ABCDE cluster but activated for phosphorylation of other targets. In contrast, DNA hairpin ends promote cis-autophosphorylation. Phosphorylation of four Thr residues in ABCDE leads to gross structural rearrangement of DNA-PK, widening the DNA binding groove for Artemis recruitment and hairpin cleavage. Meanwhile, Artemis locks DNA-PK into the kinase-inactive state. Kinase activity and autophosphorylation of DNA-PK are regulated by different DNA ends, feeding forward to coordinate NHEJ events.
External linksMol Cell / PubMed:34936881 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 4.4 Å
Structure data

EMDB-25110:
CryoEM map of DNA-PK complex VIb with AMPPNP
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-25111:
CryoEM map of DNA-PK complex VIIb with AMPPNP
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-25112:
CryoEM map of DNA-PK complex VIIa with AMPPNP
Method: EM (single particle) / Resolution: 4.2 Å

25113

7sgl

EMDB-25113, PDB-7sgl:
DNA-PK complex of DNA end processing
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-25114:
FATKIN domain of the phosphorylated DNA-PKcs
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-25115:
KU, Artemis, DNA and DNA-PKcs_Nheat in the NHEJ DNA end processing complex
Method: EM (single particle) / Resolution: 2.9 Å

25439

7su3

EMDB-25439, PDB-7su3:
CryoEM structure of DNA-PK complex VII
Method: EM (single particle) / Resolution: 3.3 Å

25440

7sud

EMDB-25440, PDB-7sud:
CryoEM structure of DNA-PK complex VIII
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE / Phytic acid

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • Human (human)
  • synthetic construct (others)
  • escherichia coli (E. coli)
KeywordsDNA BINDING PROTEIN/DNA / endonuclease / Kinase / complex / DNA BINDING PROTEIN / TRANSFERASE / DNA BINDING PROTEIN-DNA complex / NHEJ / DNA-PK / DNA repair

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