A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2.

ABSTRACT: Yeast Dre2 is an essential Fe-S cluster-containing protein that has been implicated in cytosolic Fe-S protein biogenesis and in cell death regulation in response to oxidative stress. Its absence in yeast can be complemented by the human homologous antiapoptotic protein cytokine-induced apoptosis inhibitor 1 (also known as anamorsin), suggesting at least one common function. Using complementary techniques, we have investigated the biochemical and biophysical properties of Dre2. We show that it contains an N-terminal domain whose structure in solution consists of a stable well-structured monomer with an overall typical S-adenosylmethionine methyltransferase fold lacking two α-helices and a β-strand. The highly conserved C-terminus of Dre2, containing two Fe-S clusters, influences the flexibi

SUBMITTER: Soler N 

PROVIDER: S-EPMC3440578 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature