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TitleRNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment.
Journal, issue, pagesJ Biol Chem, Vol. 291, Issue 18, Page 9396-9410, Year 2016
Publish dateApr 29, 2016
AuthorsCurtis D Hodge / Ismail H Ismail / Ross A Edwards / Greg L Hura / Andrew T Xiao / John A Tainer / Michael J Hendzel / J N Mark Glover /
PubMed AbstractDNA double strand break (DSB) responses depend on the sequential actions of the E3 ubiquitin ligases RNF8 and RNF168 plus E2 ubiquitin-conjugating enzyme Ubc13 to specifically generate histone Lys-63- ...DNA double strand break (DSB) responses depend on the sequential actions of the E3 ubiquitin ligases RNF8 and RNF168 plus E2 ubiquitin-conjugating enzyme Ubc13 to specifically generate histone Lys-63-linked ubiquitin chains in DSB signaling. Here, we defined the activated RNF8-Ubc13∼ubiquitin complex by x-ray crystallography and its functional solution conformations by x-ray scattering, as tested by separation-of-function mutations imaged in cells by immunofluorescence. The collective results show that the RING E3 RNF8 targets E2 Ubc13 to DSB sites and plays a critical role in damage signaling by stimulating polyubiquitination through modulating conformations of ubiquitin covalently linked to the Ubc13 active site. Structure-guided separation-of-function mutations show that the RNF8 E2 stimulating activity is essential for DSB signaling in mammalian cells and is necessary for downstream recruitment of 53BP1 and BRCA1. Chromatin-targeted RNF168 rescues 53BP1 recruitment involved in non-homologous end joining but not BRCA1 recruitment for homologous recombination. These findings suggest an allosteric approach to targeting the ubiquitin-docking cleft at the E2-E3 interface for possible interventions in cancer and chronic inflammation, and moreover, they establish an independent RNF8 role in BRCA1 recruitment.
External linksJ Biol Chem / PubMed:26903517 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution8.3 Å
Structure data

SASDBR3:
Wild type RNF8 complexed with Ubc13 (C87K, K92A mutant): conjugated to Ubiquitin
Method: SAXS/SANS

SASDBS3:
Wild type RNF8 complexed with Ubc13 (C87K, K92A mutant) and Mms2: conjugated to Ubiquitin
Method: SAXS/SANS

SASDBT3:
RNF8 (L451D mutant) complexed with Ubc13 (C87K, K92A mutant): conjugated to Ubiquitin
Method: SAXS/SANS

SASDBU3:
RNF8 (L451D mutant) complexed with Ubc13 (C87K, K92A mutant) and Mms2: conjugated to Ubiquitin
Method: SAXS/SANS

PDB-4whv:
E3 ubiquitin-protein ligase RNF8 in complex with Ubiquitin-conjugating enzyme E2 N and Polyubiquitin-B
Method: X-RAY DIFFRACTION / Resolution: 8.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
Keywordsligase/protein binding / E3 ligase / E2 conjugating enzyme / ubiquitination / coiled coil / ligase-protein binding complex

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