This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fukumoto, Y.
Right arrow Articles by Hanaoka, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fukumoto, Y.
Right arrow Articles by Hanaoka, F.

 Previous Article  |  Next Article 

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.

Schizosaccharomyces pombe Ddb1 Recruits Substrate-Specific Adaptor Proteins through a Novel Protein Motif, the DDB-Box{triangledown} ,{dagger}

Yasunori Fukumoto,1,2,{ddagger} 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.


* Corresponding author. Present address: Faculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo 171-8588, Japan. Phone: 81 (3) 3986-0221. Fax: 81 (3) 5992-1029. E-mail: fumio.hanaoka{at}gakushuin.ac.jp

{triangledown} Published ahead of print on 15 September 2008.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{ddagger} Present address: Department of Molecular Cell Biology, Graduate School of Pharmaceutical Sciences, Chiba University, Inohana 1-8-1, Chuo-ku, Chiba 260-8675, Japan.


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.