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TitleRecognition of BACH1 quaternary structure degrons by two F-box proteins under oxidative stress.
Journal, issue, pagesCell, Vol. 187, Issue 26, Page 7568-7584.e22, Year 2024
Publish dateDec 26, 2024
AuthorsShiyun Cao / Sheena Faye Garcia / Huigang Shi / Ellie I James / Yuki Kito / Hui Shi / Haibin Mao / Sharon Kaisari / Gergely Rona / Sophia Deng / Hailey V Goldberg / Jackeline Ponce / Beatrix Ueberheide / Luca Lignitto / Miklos Guttman / Michele Pagano / Ning Zheng /
PubMed AbstractUbiquitin-dependent proteolysis regulates diverse cellular functions with high substrate specificity, which hinges on the ability of ubiquitin E3 ligases to decode the targets' degradation signals, i. ...Ubiquitin-dependent proteolysis regulates diverse cellular functions with high substrate specificity, which hinges on the ability of ubiquitin E3 ligases to decode the targets' degradation signals, i.e., degrons. Here, we show that BACH1, a transcription repressor of antioxidant response genes, features two distinct unconventional degrons encrypted in the quaternary structure of its homodimeric BTB domain. These two degrons are both functionalized by oxidative stress and are deciphered by two complementary E3s. FBXO22 recognizes a degron constructed by the BACH1 BTB domain dimer interface, which is unmasked from transcriptional co-repressors after oxidative stress releases BACH1 from chromatin. When this degron is impaired by oxidation, a second BACH1 degron manifested by its destabilized BTB dimer is probed by a pair of FBXL17 proteins that remodels the substrate into E3-bound monomers for ubiquitination. Our findings highlight the multidimensionality of protein degradation signals and the functional complementarity of different ubiquitin ligases targeting the same substrate.
External linksCell / PubMed:39504958 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 5.6 Å
Structure data

42049

8ua3

EMDB-42049, PDB-8ua3:
Cryo-EM Structure of FBOX22-BACH1BTB
Method: EM (single particle) / Resolution: 3.8 Å

42051

8ua6

EMDB-42051, PDB-8ua6:
Cryo-EM Structure of SCF-FBOX22-BACH1BTB
Method: EM (single particle) / Resolution: 3.9 Å

42064

8uah

EMDB-42064, PDB-8uah:
Structure of BACH1 BTB domain-bound FBXL17 ubiquitin ligase
Method: EM (single particle) / Resolution: 3.3 Å

42102

8ubt

EMDB-42102, PDB-8ubt:
Structure of SCF-FBXL17-BACH1BTB E3 ligase complex
Method: EM (single particle) / Resolution: 3.1 Å

42105

8ubu

EMDB-42105, PDB-8ubu:
Cryo-EM structure of dimeric SCF-FBXL17-BACH1BTB E3 ligase complex close conformation
Method: EM (single particle) / Resolution: 4.6 Å

42106

8ubv

EMDB-42106, PDB-8ubv:
Cryo-EM structure of dimeric FBXL17-BACH1BTB E3 ubiquitin ligase complex
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-42115: Cryo-EM structure of dimeric SCF-FBXL17-BACH1BTB open conformation
Method: EM (single particle) / Resolution: 5.6 Å

Source
  • homo sapiens (human)
KeywordsLIGASE / F-box protein / FBXO22 / BACH1 / SCF / FBXL17 / E3 ligase / CUL1 / Cullin

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