| Title | Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 forms a nuclear E3 ubiquitin ligase with DDB1 and CUL4 that is involved in multiple plant developmental processes |
| Authors | Zhang, Yu Feng, Suhua Chen, Fangfang Chen, Haodong Wang, Jia McCall, Chad Xiong, Yue Deng, Xing Wang |
| Affiliation | Peking Univ, Coll Life Sci, Peking Yale Joint Ctr Plant Mol Genet & Agrobiote, Beijing 100871, Peoples R China. Natl Inst Biol Sci, Beijing 102206, Peoples R China. Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA. Peking Union Med Coll, Beijing 100730, Peoples R China. Beijing Normal Univ, Coll Life Sci, Beijing 100875, Peoples R China. Univ N Carolina, Program Mol Biol & Biotechnol, Dept Biochem & Biophys, Lineberger Comprehens Canc Ctr, Chapel Hill, NC 27599 USA. |
| Keywords | DNA-BINDING PROTEIN PROTEASOME PROTEOLYTIC PATHWAY DAMAGED DNA COP9 COMPLEX CELL-CYCLE VPR FUNCTION GENE DEGRADATION INTERACTS MECHANISM |
| Issue Date | 2008 |
| Publisher | plant cell |
| Citation | PLANT CELL.2008,20,(6),1437-1455. |
| Abstract | The human DDB1-CUL4 ASSOCIATED FACTOR ( DCAF) proteins have been reported to interact directly with UV-DAMAGED DNA BINDING PROTEIN1 (DDB1) through the WDxR motif in their WD40 domain and function as substrate-recognition receptors for CULLIN4-based E3 ubiquitin ligases. Here, we identified and characterized a homolog of human DCAF1/VprBP in Arabidopsis thaliana. Yeast two-hybrid analysis demonstrated the physical interaction between DCAF1 and DDB1 from Arabidopsis, which is likely mediated via the WD40 domain of DCAF1 that contains two WDxR motifs. Moreover, coimmunoprecipitation assays showed that DCAF1 associates with DDB1, RELATED TO UBIQUITIN-modified CUL4, and the COP9 signalosome in vivo but not with CULLIN-ASSOCIATED and NEDDYLATION-DISSOCIATED1, CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1), or the COP10-DET1-DDB1 complex, supporting the existence of a distinct Arabidopsis CUL4 E3 ubiquitin ligase, the CUL4-DDB1-DCAF1 complex. Transient expression of fluorescently tagged DCAF1, DDB1, and CUL4 in onion epidermal cells showed their colocalization in the nucleus, consistent with the notion that the CUL4-DDB1-DCAF1 complex functions as a nuclear E3 ubiquitin ligase. Genetic and phenotypic analysis of two T-DNA insertion mutants of DCAF1 showed that embryonic development of the dcaf1 homozygote is arrested at the globular stage, indicating that DCAF1 is essential for plant embryogenesis. Reducing the levels of DCAF1 leads to diverse developmental defects, implying that DCAF1 might be involved in multiple developmental pathways. |
| URI | http://hdl.handle.net/20.500.11897/162619 |
| ISSN | 1040-4651 |
| DOI | 10.1105/tpc.108.058891 |
| Indexed | SCI(E) PubMed |
| Appears in Collections: | 生命科学学院 |
