Soler N, et al. (2012) A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2. FEBS J 279(12):2108-19
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 a-helices and a ?-strand. The highly conserved C-terminus of Dre2, containing two Fe-S clusters, influences the flexibility of the N-terminal domain. We discuss the hypotheses that the activity of the N-terminal domain could be modulated by the redox activity of Fe-S clusters containing the C-terminus domain in vivo.
|Status: Published||Type: Journal Article | Research Support, Non-U.S. Gov't||PubMed ID: 22487307|
Topics addressed in this paper
- To go to the Locus page for a gene, click on the gene name.
|Fungal Related Genes/Proteins|
|Protein Sequence Features|
|Protein/Nucleic Acid Structure|