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  A DNA-Dependent Protease Involved in DNA-Protein Crosslink Repair

Stingele, J., Schwarz, M. S., Bloemeke, N., Wolf, P. G., & Jentsch, S. (2014). A DNA-Dependent Protease Involved in DNA-Protein Crosslink Repair. CELL, 158(2), 327-338. doi:10.1016/j.cell.2014.04.053.

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 Creators:
Stingele, Julian1, Author              
Schwarz, Michael S.1, Author              
Bloemeke, Nicolas1, Author              
Wolf, Peter G.1, Author              
Jentsch, Stefan1, Author              
Affiliations:
1Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              

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Free keywords: NUCLEOTIDE EXCISION-REPAIR; YEAST SACCHAROMYCES-CEREVISIAE; ANTITUMOR DRUG CAMPTOTHECIN; TARGETED UBIQUITIN LIGASE; TOPOISOMERASE-I; HOMOLOGOUS RECOMBINATION; TRANSLESION SYNTHESIS; DAMAGE TOLERANCE; DVC1 C1ORF124; PATHWAY
 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 uponDPCs, 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.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: CELL
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 158 (2) Sequence Number: - Start / End Page: 327 - 338 Identifier: ISSN: 0092-8674