Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1.

ABSTRACT:

Aims

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.

Results

Our data identify a redox-regulated monomer-dimer equilibrium of YchF as a key event in the functional cycle of YchF. Upon oxidative stress, the oxidation of a conserved and surface-exposed cysteine residue promotes YchF dimerization, whic

SUBMITTER: Hannemann L 

PROVIDER: S-EPMC4742990 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature