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Mol Cell Biol. 2008 Nov;28(22):6746-56. doi: 10.1128/MCB.00757-08. Epub 2008 Sep 15.

Schizosaccharomyces pombe Ddb1 recruits substrate-specific adaptor proteins through a novel protein motif, the DDB-box.

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  • 1Faculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo 171-8588, Japan.


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.

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