Acetylation Regulates Thioredoxin Reductase Oligomerization and Activity.

ABSTRACT:

Aims

Thioredoxin reductase 1 (TrxR1) is a cancer target and essential selenoprotein that defends the cell against reactive oxygen species and regulates cellular signaling and redox pathways. Previous cell-based studies correlated TrxR1 acetylation with modulated cellular reduction activity, yet the function of specific acetylation sites on TrxR1 remains unknown.

Innovation

We produced site-specifically acetylated TrxR1 variants that also contain selenocysteine (Sec). We demonstrated efficient high-fidelity protein synthesis with 22 different amino acids by simultaneous UAG codon reassignment to N_ɛ-acetyl-lysine and UGA codon recoding to Sec.

Results

We characterized TrxR1 variants acetylated at physiologically relevant sites and found that single acetylatio

SUBMITTER: Wright DE 

PROVIDER: S-EPMC6025699 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature