Premium
The conserved factor DE‐ETIOLATED 1 cooperates with CUL4–DDB1 DDB2 to maintain genome integrity upon UV stress
Author(s) -
Castells Enric,
Molinier Jean,
Benvenuto Giovanna,
Bourbousse Clara,
Zabulon Gerald,
Zalc Antoine,
Cazzaniga Stefano,
Genschik Pascal,
Barneche Fredy,
Bowler Chris
Publication year - 2011
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2011.20
Subject(s) - biology , etiolation , genetics , ddb1 , genome , microbiology and biotechnology , dna binding protein , transcription factor , gene , biochemistry , enzyme
Plants and many other eukaryotes can make use of two major pathways to cope with mutagenic effects of light, photoreactivation and nucleotide excision repair (NER). While photoreactivation allows direct repair by photolyase enzymes using light energy, NER requires a stepwise mechanism with several protein complexes acting at the levels of lesion detection, DNA incision and resynthesis. Here we investigated the involvement in NER of DE‐ETIOLATED 1 (DET1), an evolutionarily conserved factor that associates with components of the ubiquitylation machinery in plants and mammals and acts as a negative repressor of light‐driven photomorphogenic development in Arabidopsis. Evidence is provided that plant DET1 acts with CULLIN4‐based ubiquitin E3 ligase, and that appropriate dosage of DET1 protein is necessary for efficient removal of UV photoproducts through the NER pathway. Moreover, DET1 is required for CULLIN4‐dependent targeted degradation of the UV‐lesion recognition factor DDB2. Finally, DET1 protein is degraded concomitantly with DDB2 upon UV irradiation in a CUL4‐dependent mechanism. Altogether, these data suggest that DET1 and DDB2 cooperate during the excision repair process.