Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1 | Zendy

Liya Hannemann | Zendy; Ida Suppanz | Zendy; Qiaorui Ba | Zendy; Katherine MacInnes | Zendy; Friedel Drepper | Zendy; Bettina Warscheid | Zendy; HansGeorg Koch | Zendy

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Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1

Author(s) -

Liya Hannemann,

Ida Suppanz,

Qiaorui Ba,

Katherine MacInnes,

Friedel Drepper,

Bettina Warscheid,

HansGeorg Koch

Publication year - 2015

Publication title -

antioxidants and redox signaling

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.277

H-Index - 190

eISSN - 1557-7716

pISSN - 1523-0864

DOI - 10.1089/ars.2015.6272

Subject(s) - thioredoxin , biochemistry , microbiology and biotechnology , oxidative phosphorylation , cysteine , oxidative stress , gtpase , biology , atpase , conserved sequence , chemistry , enzyme , peptide sequence , gene

YchF/Ola1 are unconventional members of the universally conserved GTPase family because they preferentially hydrolyze ATP rather than GTP. These ATPases have been associated with various cellular processes and pathologies, including DNA repair, tumorigenesis, and apoptosis. In particular, a possible role in regulating the oxidative stress response has been suggested for both bacterial and human YchF/Ola1. In this study, we analyzed how YchF responds to oxidative stress and how it potentially regulates the antioxidant response.

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