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通过紫外线交联和质谱法对大肠杆菌铁摄取调节蛋白中DNA结合位点的表征

Characterization of the DNA-binding site in the ferric uptake regulator protein from Escherichia coli by UV crosslinking and mass spectrometry.

作者信息

Tiss Ali, Barre Olivier, Michaud-Soret Isabelle, Forest Eric

机构信息

Laboratoire de Spectrométrie de Masse des Protéines, Institut de Biologie Structurale (UMR 5075 CEA-CNRS-UJF), Grenoble, France.

出版信息

FEBS Lett. 2005 Oct 24;579(25):5454-60. doi: 10.1016/j.febslet.2005.08.067. Epub 2005 Sep 23.

DOI:10.1016/j.febslet.2005.08.067
PMID:16212958
Abstract

Ferric uptake regulator protein (Fur) is activated by its cofactor iron to a state that binds to a specific DNA sequence called 'Fur box'. Using mass spectrometry-based methods, we showed that Tyr 55 of Escherichia coli Fur, as well as the two thymines in positions 18 and 19 of the consensus Fur Box, are involved with binding. A conformational model of the Fur-DNA complex is proposed, in which DNA is in contact with each H4 [A52-A64] Fur helix. We propose that this interaction is a common feature for the Fur-like proteins, such as Zur and PerR, and their respective DNA boxes.

摘要

铁摄取调节蛋白（Fur）被其辅因子铁激活至一种能与特定DNA序列“Fur盒”结合的状态。通过基于质谱的方法，我们发现大肠杆菌Fur的酪氨酸55以及Fur盒共有序列中第18和19位的两个胸腺嘧啶参与结合。我们提出了Fur-DNA复合物的构象模型，其中DNA与每个H4 [A52-A64] Fur螺旋接触。我们认为这种相互作用是Fur样蛋白（如Zur和PerR）及其各自DNA盒的共同特征。

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