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Biophysical characterization of the complex between the iron-responsive transcription factor Fep1 and DNA
European Biophysics Journal ( IF 2.2 ) Pub Date : 2021-01-04 , DOI: 10.1007/s00249-020-01489-y
Adriana E Miele 1, 2 , Laura Cervoni 1 , Aline Le Roy 3 , Antimo Cutone 4 , Giovanni Musci 4 , Christine Ebel 3 , Maria Carmela Bonaccorsi di Patti 1
Affiliation  

Fep1 is an iron-responsive GATA-type transcriptional repressor present in numerous fungi. The DNA-binding domain of this protein is characterized by the presence of two zinc fingers of the Cys2-Cys2 type and a Cys-X5-Cys-X8-Cys-X2-Cys motif located between the two zinc fingers, that is involved in binding of a [2Fe-2S] cluster. In this work, biophysical characterization of the DNA-binding domain of Pichia pastoris Fep1 and of the complex of the protein with cognate DNA has been undertaken. The results obtained by analytical ultracentrifugation sedimentation velocity, small-angle X-ray scattering and differential scanning calorimetry indicate that Fep1 is a natively unstructured protein that is able to bind DNA forming 1:1 and 2:1 complexes more compact than the individual partners. Complex formation takes place independently of the presence of a stoichiometric [2Fe-2S] cluster, suggesting that the cluster may play a role in recruiting other protein(s) required for regulation of transcription in response to changes in intracellular iron levels.



中文翻译:

铁反应转录因子 Fep1 和 DNA 之间复合物的生物物理学特征

Fep1 是一种铁反应性 GATA 型转录抑制因子,存在于多种真菌中该蛋白质的 DNA 结合域的特征在于存在两个 Cys 2 -Cys 2型锌指和位于两个锌指之间的Cys-X 5 -Cys-X 8 -Cys-X 2 -Cys 基序,这涉及 [2Fe-2S] 簇的结合。在这项工作中,毕赤酵母DNA 结合域的生物物理表征Fep1 和蛋白质与同源 DNA 的复合物的研究已经进行。通过分析超速离心沉降速度、小角度 X 射线散射和差示扫描量热法获得的结果表明,Fep1 是一种天然的非结构化蛋白质,能够与 DNA 结合形成 1:1 和 2:1 复合物,比单个伴侣更紧凑。复合物的形成与化学计量的 [2Fe-2S] 簇的存在无关,这表明该簇可能在招募其他蛋白质方面发挥作用,这些蛋白质是响应细胞内铁水平变化而调节转录所需的。

更新日期:2021-01-04
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