Schizosaccharomyces pombe Ddb1 recruits substrate-specific adaptor proteins through a novel protein motif, the DDB-box.
DDB1 was isolated as a UV-damaged DNA-binding protein, but recent studies established that it plays a role as a component of cullin 4A ubiquitin ligases. Cullin-RING complexes are the largest known ubiquitin ligase family, with hundreds of substrate-specific adaptor subunits and which are defined by characteristic motifs. A common motif ... for DDB1/cullin 4 ubiquitin ligases, a WDXR motif, was recently reported. Here, we show that Schizosaccharomyces pombe Ddb1 associates with several WD40 repeat proteins that share a novel protein motif designated the DDB-box, a motif essential for interaction with Ddb1 and independent of WD40 repeats, unlike the WDXR motif. We also show that ddb1(+) and the putative CSA homolog ckn1(+) are involved in transcription-coupled nucleotide excision repair and that the DDB-box is essential for the ckn1(+) function in vivo. These data indicate that the DDB-box is another common motif which defines adaptor proteins for DDB1/cullin 4 ubiquitin ligases.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Animals, Cell Line, DNA Damage, DNA Repair, DNA-Binding Proteins, Humans, Macromolecular Substances, Molecular Sequence Data, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Alignment, Transcription, Genetic, Ultraviolet Rays
Amino Acid Motifs, Amino Acid Sequence, Animals, Cell Line, DNA Damage, DNA Repair, DNA-Binding Proteins, Humans, Macromolecular Substances, Molecular Sequence Data, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Alignment, Transcription, Genetic, Ultraviolet Rays
Mol. Cell. Biol.
Date: Nov. 01, 2008
PubMed ID: 18794354
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