Arabidopsis cockayne syndrome A-like proteins 1A and 1B form a complex with CULLIN4 and damage DNA binding protein 1A and regulate the response to UV irradiation.
In plants, as in animals, DNA is constantly subject to chemical modification. UV-B irradiation is a major genotoxic agent and has significant effects on plant growth and development. Through forward genetic screening, we identified a UV-B-sensitive mutant (csaat1a-3) in Arabidopsis thaliana, in which expression of CSAat1A, encoding a Cockayne Syndrome ... A-like protein, is reduced due to insertion of a T-DNA in the promoter region. Arabidopsis lacking CSAat1A or its homolog CSAat1B is more sensitive to UV-B and the genotoxic drug methyl methanesulfonate and exhibits reduced transcription-coupled repair activity. Yeast two-hybrid analysis indicated that both CSAat1A and B interact with DDB1A (UV-Damage DNA Binding Protein1). Coimmunoprecipitation assays demonstrated that CSAat1A and B associate with the CULLIN4 (CUL4)-DDB1A complex in Arabidopsis. A split-yellow fluorescent protein assay showed that this interaction occurs in the nucleus, consistent with the idea that the CUL4-DDB1A-CSA complex functions as a nuclear E3 ubiquitin ligase. CSAat1A and B formed heterotetramers in Arabidopsis. Taken together, our data suggest that the plant CUL4-DDB1A(CSAat1A and B) complex represents a unique mechanism to promote ubiquitination of substrates in response to DNA damage.
Mesh Terms:
Arabidopsis, Arabidopsis Proteins, Base Sequence, Biological Transport, Active, DNA Primers, Genes, Plant, Indoleacetic Acids, Lactones, Membrane Transport Proteins, Mutation, Phenotype, Plant Growth Regulators, Plant Shoots, Plants, Genetically Modified, Xylem
Arabidopsis, Arabidopsis Proteins, Base Sequence, Biological Transport, Active, DNA Primers, Genes, Plant, Indoleacetic Acids, Lactones, Membrane Transport Proteins, Mutation, Phenotype, Plant Growth Regulators, Plant Shoots, Plants, Genetically Modified, Xylem
Plant Cell
Date: Jul. 01, 2010
PubMed ID: 20622147
View in: Pubmed Google Scholar
Download Curated Data For This Publication
102680
Switch View:
- Interactions 9