Redox state and the sirtuin deacetylases are major factors that regulate the acetylation status of the stress protein NQO1.

ABSTRACT: The stress induced protein NQO1 can participate in a wide range of biological pathways which are dependent upon the interaction of NQO1 with protein targets. Many of the protein-protein interactions involving NQO1 have been shown to be regulated by the pyridine nucleotide redox balance. NQO1 can modify its conformation as a result of redox changes in pyridine nucleotides and sites on the C-terminal and helix seven regions of NQO1 have been identified as potential areas that may be involved in redox-dependent protein-protein interactions. Since post-translational modifications can modify the functionality of proteins, we examined whether redox-dependent conformational changes induced in NQO1 would alter lysine acetylation. Recombinant NQO1 was incubated with and without NADH then acetylated

SUBMITTER: Siegel D 

PROVIDER: S-EPMC9667027 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature