Academic Journal

Wss1 metalloprotease partners with Cdc48/Doa1 in processing genotoxic SUMO conjugates

التفاصيل البيبلوغرافية
العنوان: Wss1 metalloprotease partners with Cdc48/Doa1 in processing genotoxic SUMO conjugates
المؤلفون: Maxim Y Balakirev, James E Mullally, Adrien Favier, Nicole Assard, Eric Sulpice, David F Lindsey, Anastasia V Rulina, Xavier Gidrol, Keith D Wilkinson
المصدر: eLife, Vol 4 (2015)
بيانات النشر: eLife Sciences Publications Ltd, 2015.
سنة النشر: 2015
المجموعة: LCC:Medicine
LCC:Science
LCC:Biology (General)
مصطلحات موضوعية: SUMO metabolism, DNA repair, poly SUMO, Cdc48, Doa1, vacuole, Medicine, Science, Biology (General), QH301-705.5
الوصف: Sumoylation during genotoxic stress regulates the composition of DNA repair complexes. The yeast metalloprotease Wss1 clears chromatin-bound sumoylated proteins. Wss1 and its mammalian analog, DVC1/Spartan, belong to minigluzincins family of proteases. Wss1 proteolytic activity is regulated by a cysteine switch mechanism activated by chemical stress and/or DNA binding. Wss1 is required for cell survival following UV irradiation, the smt3-331 mutation and Camptothecin-induced formation of covalent topoisomerase 1 complexes (Top1cc). Wss1 forms a SUMO-specific ternary complex with the AAA ATPase Cdc48 and an adaptor, Doa1. Upon DNA damage Wss1/Cdc48/Doa1 is recruited to sumoylated targets and catalyzes SUMO chain extension through a newly recognized SUMO ligase activity. Activation of Wss1 results in metalloprotease self-cleavage and proteolysis of associated proteins. In cells lacking Tdp1, clearance of topoisomerase covalent complexes becomes SUMO and Wss1-dependent. Upon genotoxic stress, Wss1 is vacuolar, suggesting a link between genotoxic stress and autophagy involving the Doa1 adapter.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2050-084X
Relation: https://elifesciences.org/articles/06763; https://doaj.org/toc/2050-084X
DOI: 10.7554/eLife.06763
URL الوصول: https://doaj.org/article/1d2327de45b944ef8e8e73046a85a414
رقم الانضمام: edsdoj.1d2327de45b944ef8e8e73046a85a414
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:2050084X
DOI:10.7554/eLife.06763