4.6 Article

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

期刊

FEBS JOURNAL
卷 279, 期 12, 页码 2108-2119

出版社

WILEY-BLACKWELL
DOI: 10.1111/j.1742-4658.2012.08597.x

关键词

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

资金

  1. CNRS
  2. INSERM
  3. Institut Curie
  4. Medical Research Council [MC_U117584256] Funding Source: researchfish
  5. MRC [MC_U117584256] Funding Source: UKRI

向作者/读者索取更多资源

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 .

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