A Rad26–Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage

Elies C. Woudstra, Chris Gilbert, Jane Fellows, Lars Jansen, Jaap Brouwer, Hediye Erdjument-Bromage, Paul Tempst and Jesper Q. Svejstrup ()
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Elies C. Woudstra: Mechanisms of Gene Transcription Laboratory, Cancer Research UK, Clare Hall Laboratories
Chris Gilbert: Mechanisms of Gene Transcription Laboratory, Cancer Research UK, Clare Hall Laboratories
Jane Fellows: Mechanisms of Gene Transcription Laboratory, Cancer Research UK, Clare Hall Laboratories
Lars Jansen: Leiden Institute of Chemistry, Leiden University
Jaap Brouwer: Leiden Institute of Chemistry, Leiden University
Hediye Erdjument-Bromage: Molecular Biology Programme, Memorial Sload-Kettering Cancer Center
Paul Tempst: Molecular Biology Programme, Memorial Sload-Kettering Cancer Center
Jesper Q. Svejstrup: Mechanisms of Gene Transcription Laboratory, Cancer Research UK, Clare Hall Laboratories

Nature, 2002, vol. 415, issue 6874, 929-933

Abstract: Abstract Eukaryotic cells use multiple, highly conserved mechanisms to contend with ultraviolet-light-induced DNA damage1. One important response mechanism is transcription-coupled repair (TCR), during which DNA lesions in the transcribed strand of an active gene are repaired much faster than in the genome overall2. In mammalian cells, defective TCR gives rise to the severe human disorder Cockayne's syndrome (CS)3. The best-studied CS gene, CSB, codes for a Swi/Snf-like DNA-dependent ATPase, whose yeast homologue is called Rad26 (ref. 4). Here we identify a yeast protein, termed Def1, which forms a complex with Rad26 in chromatin. The phenotypes of cells lacking DEF1 are consistent with a role for this factor in the DNA damage response, but Def1 is not required for TCR. Rather, def1 cells are compromised for transcript elongation, and are unable to degrade RNA polymerase II (RNAPII) in response to DNA damage. Our data suggest that RNAPII stalled at a DNA lesion triggers a coordinated rescue mechanism that requires the Rad26–Def1 complex, and that Def1 enables ubiquitination and proteolysis of RNAPII when the lesion cannot be rapidly removed by Rad26-promoted DNA repair.

Date: 2002
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DOI: 10.1038/415929a

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