title: 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 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.
authors.affiliation: CNRS UMR2027, Centre Universitaire, Orsay, France.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Soler
authors.forename: Constantin T
authors.initials: CT
authors.lastname: Craescu
authors.forename: Jacques
authors.initials: J
authors.lastname: Gallay
authors.forename: Yves-Michel
authors.initials: YM
authors.lastname: Frapart
authors.forename: Daniel
authors.initials: D
authors.lastname: Mansuy
authors.forename: Bertrand
authors.initials: B
authors.lastname: Raynal
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Baldacci
authors.forename: Annalisa
authors.initials: A
authors.lastname: Pastore
authors.forename: Meng-Er
authors.initials: ME
authors.lastname: Huang
authors.forename: Laurence
authors.initials: L
authors.lastname: Vernis
mesh_terms: D000595:Amino Acid Sequence; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
chemical_list: C531900:Dre2 protein, S cerevisiae; D007506:Iron-Sulfur Proteins; D029701:Saccharomyces cerevisiae Proteins