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| DNA Repair (Amst.) Jun (2008); 7(6):858-68 | |
| The NER protein Rad33 shows functional homology to human Centrin2 and is involved in modification of Rad4- | |
| den Dulk B, van Eijk P, de Ruijter M, Brandsma JA, Brouwer J | |
| MGC Department of Molecular Genetics, Leiden Institute of Chemistry, Leiden University, PO Box 9502, 2300 RA Leiden, The Netherlands- | |
| Abstract: In the yeast Saccharomyces cerevisiae the Rad4-Rad23 complex is implicated in the initial damage recognition of the Nucleotide Excision Repair -NER- pathway- NER removes a variety of lesions via two subpathways- Transcription Coupled Repair -TCR- and Global Genome Repair -GGR-- We previously showed that the new NER protein Rad33 is involved in both NER subpathways TCR and GGR- In the present study we show UV induced modification of Rad4 that is strongly increased in cells deleted for RAD33- Modification of Rad4 in rad33 cells does not require the incision reaction but is dependent on the TCR factor Rad26- The predicted structure of Rad33 shows resemblance to the Centrin homologue Cdc31- In human cells, Centrin2 binds to XPC and is involved in NER- We demonstrate that Rad4 binds Rad33 directly and via the same conserved amino acids required for the interaction of XPC with Centrin2- Disruption of the Rad4-Rad33 interaction is sufficient to enhance the modification of Rad4 and results in a repair defect similar to that of a rad33 mutant- The current study suggests that the role of Rad33 in the Rad4-Rad23 complex might have parallels with the role of Centrin2 in the XPC-HHR23B complex- | |
| [PUBMED: 18387345] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |