A DNA-dependent protease involved in DNA-protein crosslink repair.

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

Cell

journal_title

Cell

authors

Stingele J,Schwarz MS,Bloemeke N,Wolf PG,Jentsch S

doi

10.1016/j.cell.2014.04.053

subject

Has Abstract

pub_date

2014-07-17 00:00:00

pages

327-338

issue

2

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(14)00746-6

journal_volume

158

pub_type

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