@article{9377e8779c914949b2d0c605771d325b,
title = "Wss1 Promotes Replication Stress Tolerance by Degrading Histones",
abstract = "Maddi et al. show that Wss1 degrades unincorporated histones to tolerate replication stress. Wss1 is a DNA-dependent metalloprotease that cleaves DNA-protein crosslinks to maintain genome stability. Unlike DNA-protein crosslink removal, Wss1 does not require interactions with Sumo or Cdc48 to act on histones that bind non-specifically to DNA.",
keywords = "Ddi1, DNA-protein crosslinks, histone H2A, histone H3, histone H4, HU, hydroxyurea, metalloprotease, Rad51, replication stress, Wss1",
author = "Karthik Maddi and Sam, {Daniel Kwesi} and Florian Bonn and Stefan Prgomet and Eric Tulowetzke and Masato Akutsu and Jaime Lopez-Mosqueda and Ivan Dikic",
note = "Funding Information: We are grateful to the late Susan Lindquist for providing plasmids, Akash Gunjan for providing the histone-reduced yeast strain ( hht2-hhf2Δ ), and Helle Ulrich for providing Rad53 mutant yeast strains. We thank Dikic lab members for their continued support and constructive discussions. J.L.-M. was supported by a long-term post-doctoral fellowship from the Human Frontiers Science Program and the South Dakota Agricultural Experiment Station . D.K.S. is supported by South Dakota Agricultural Experiment Station funds. This work was supported by grants SFB1177 and SFB1361 from the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) to I.D. Publisher Copyright: {\textcopyright} 2020 The Authors",
year = "2020",
month = mar,
day = "3",
doi = "10.1016/j.celrep.2020.02.018",
language = "English",
volume = "30",
pages = "3117--3126.e4",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "9",
}