Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function.

ABSTRACT: Erv1 is an FAD-dependent thiol oxidase of the ERV (essential for respiration and viability)/ALR (augmenter of liver regeneration) sub-family and an essential component of the mitochondrial import and assembly pathway. Erv1 contains six tryptophan residues, which are all located in the highly conserved C-terminal FAD-binding domain. Though important structural roles were predicted for the invariable Trp(95), no experimental study has been reported. In the present study, we investigated the structural and functional roles of individual tryptophan residues of Erv1. Six single tryptophan-to-phenylalanine yeast mutant strains were generated and their effects on cell viability were tested at various temperatures. Then, the mutants were purified from Escherichia coli. Their effects on folding, FA

SUBMITTER: Wang Q 

PROVIDER: S-EPMC4721541 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature