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Molecular and Cellular Biology, November 2008, p. 6746-6756, Vol. 28, No. 22
0270-7306/08/$08.00+0 doi:10.1128/MCB.00757-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
,
Naoshi Dohmae,3 and
Fumio Hanaoka1,2*
Graduate School of Frontier Biosciences, Osaka University, and Solution Oriented Research for Science and Technology (SORST), Japan Science and Technology Agency, 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan,1 Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamada-oka, Suita, Osaka 565-0871, Japan,2 Biomolecular Characterization Team, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan3
Received 10 May 2008/ Returned for modification 22 July 2008/ Accepted 8 September 2008
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.
Published ahead of print on 15 September 2008.
Supplemental material for this article may be found at http://mcb.asm.org/.
Present address: Department of Molecular Cell Biology, Graduate School of Pharmaceutical Sciences, Chiba University, Inohana 1-8-1, Chuo-ku, Chiba 260-8675, Japan.
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