Abstract:
:Toxic DNA-protein crosslinks (DPCs) arise by ionizing irradiation and UV light, are particularly caused by endogenously produced reactive compounds such as formaldehyde, and also occur during compromised topoisomerase action. Although nucleotide excision repair and homologous recombination contribute to cell survival upon DPCs, hardly anything is known about mechanisms that target the protein component of DPCs directly. Here, we identify the metalloprotease Wss1 as being crucial for cell survival upon exposure to formaldehyde and topoisomerase 1-dependent DNA damage. Yeast mutants lacking Wss1 accumulate DPCs and exhibit gross chromosomal rearrangements. Notably, in vitro assays indicate that substrates such as topoisomerase 1 are processed by the metalloprotease directly and in a DNA-dependent manner. Thus, our data suggest that Wss1 contributes to survival of DPC-harboring cells by acting on DPCs proteolytically. We propose that DPC proteolysis enables repair of these unique lesions via downstream canonical DNA repair pathways.
journal_name
Celljournal_title
Cellauthors
Stingele J,Schwarz MS,Bloemeke N,Wolf PG,Jentsch Sdoi
10.1016/j.cell.2014.04.053subject
Has Abstractpub_date
2014-07-17 00:00:00pages
327-338issue
2eissn
0092-8674issn
1097-4172pii
S0092-8674(14)00746-6journal_volume
158pub_type
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