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Schizosaccharomyces Pombe Ddb1 Recruits Substrate-specific Adaptor Proteins Through a Novel Protein Motif, the DDB-box

Overview
Journal Mol Cell Biol
Specialty Cell Biology
Date 2008 Sep 17
PMID 18794354
Citations 10
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Abstract

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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References
1.
Cardozo T, Pagano M . The SCF ubiquitin ligase: insights into a molecular machine. Nat Rev Mol Cell Biol. 2004; 5(9):739-51. DOI: 10.1038/nrm1471. View

2.
Tsai T, Lee Y, Hsiao W, Tsao Y, Chen S . NRIP, a novel nuclear receptor interaction protein, enhances the transcriptional activity of nuclear receptors. J Biol Chem. 2005; 280(20):20000-9. DOI: 10.1074/jbc.M412169200. View

3.
Li S, Smerdon M . Rpb4 and Rpb9 mediate subpathways of transcription-coupled DNA repair in Saccharomyces cerevisiae. EMBO J. 2002; 21(21):5921-9. PMC: 131086. DOI: 10.1093/emboj/cdf589. View

4.
Huibregtse J, Yang J, Beaudenon S . The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc Natl Acad Sci U S A. 1997; 94(8):3656-61. PMC: 20496. DOI: 10.1073/pnas.94.8.3656. View

5.
Bontron S, Leupin O, Strubin M . Hepatitis B virus X protein interferes with cell viability through interaction with the p127-kDa UV-damaged DNA-binding protein. Virology. 2001; 287(2):266-74. DOI: 10.1006/viro.2001.1036. View