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

作者：Soler Nicolas; Craescu Constantin T; Gallay Jacques; Frapart Yves Michel; Mansuy Daniel; Raynal Bertrand; Baldacci Giuseppe; Pastore Annalisa; Huang Meng Er; Vernis Laurence^*

来源：FEBS Journal, 2012, 279(12): 2108-2119.

DOI：10.1111/j.1742-4658.2012.08597.x

• Dre2
• iron-sulfur cluster
• NMR
• SAM methyltransferase fold
• yeast

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 beta-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. Database Structural data have been deposited in the Protein Data Bank under accession number .

• 出版日期2012-6
• 单位河北医科大学