A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2.
A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2.
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DOI：
10.1111/j.1742-4658.2012.08597.x
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发表时间：
2012-06
期刊：
影响因子：
--
通讯作者：
Vernis L
中科院分区：
文献类型：
--
作者：
Soler N;Craescu CT;Gallay J;Frapart YM;Mansuy D;Raynal B;Baldacci G;Pastore A;Huang ME;Vernis L
酵母DRE2是一种重要的含Fe-S簇的蛋白质，参与了胞内Fe-S蛋白的生物发生和氧化应激对细胞死亡的调控。它在酵母中的缺失可以被人类同源抗凋亡蛋白细胞因子诱导的凋亡抑制因子1(也称为anamorsin)所补充，这表明至少有一种共同的功能。利用互补技术，我们对Dre2的生化和生物物理性质进行了研究。我们发现它含有一个N-末端结构域，其在溶液中的结构由一个稳定的、结构良好的单体组成，该单体具有一个典型的S-腺苷甲硫氨酸甲基转移酶折叠，缺少两个α-螺旋和一个β-链。DRA2的C-末端高度保守，含有两个Fe-S簇，影响了N-末端结构域的灵活性。我们讨论了N-末端结构域的活性可能受体内含C-末端结构域的Fe-S簇的氧化还原活性调节的假说。
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.
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影响因子：
15
作者：
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DOI：
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发表时间：
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影响因子：
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通讯作者：
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DOI：
10.1016/0005-2795(78)90509-3
发表时间：
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期刊：
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子：
--
作者：
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通讯作者：
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