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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Publication : The FEBS journal

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The FEBS journal - 09 May 2012

Soler N, Craescu CT, Gallay J, Frapart YM, Mansuy D, Raynal B, Baldacci G, Pastore A, Huang ME, Vernis L

Link to Pubmed [PMID] – 22487307

FEBS J. 2012 Jun;279(12):2108-19

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.

https://www.ncbi.nlm.nih.gov/pubmed/22487307