Cooperative DNA-binding and sequence-recognition mechanism of aristaless and clawless
Cooperative DNA-binding and sequence-recognition mechanism of aristaless and clawless
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DOI：
10.1038/emboj.2010.53
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发表时间：
2010-05-05
期刊：
影响因子：
11.4
通讯作者：
Tanokura, Masaru
中科院分区：
文献类型：
--
作者：
Miyazono, Ken-ichi;Zhi, Yuehua;Tanokura, Masaru
为了实现精确的基因调控，一些同源结构域蛋白协同结合DNA以增加这些位点特异性。我们报告了一个三元复合物结构，包含两个同源结构域蛋白，无芒（Al）和无爪（Cll），结合到DNA。我们的研究结果表明，扩展的保守序列的Cll同源结构域是必不可少的合作DNA结合。在Al-Cll-DNA复合物结构中，延伸区域中的残基不仅用于两个同源结构域蛋白质之间的分子间接触，而且用于通过直接相互作用的DNA的序列识别机制。延伸的N-末端臂中的残基位于DNA的小沟内以形成与碱基的直接相互作用，而同源结构域的C-末端的延伸的保守区域与Al相互作用以稳定和定位Cll同源结构域的第三个α螺旋。这种结构表明同源结构域蛋白质的协同性的一种新模式。The EMBO Journal（2010）29，1613-1623. doi：10.1038/doj.2010.53; 2010年4月13日在线发布
To achieve accurate gene regulation, some homeodomain proteins bind cooperatively to DNA to increase those site specificities. We report a ternary complex structure containing two homeodomain proteins, aristaless (Al) and clawless (Cll), bound to DNA. Our results show that the extended conserved sequences of the Cll homeodomain are indispensable to cooperative DNA binding. In the Al-Cll-DNA complex structure, the residues in the extended regions are used not only for the intermolecular contacts between the two homeodomain proteins but also for the sequence-recognition mechanism of DNA by direct interactions. The residues in the extended N-terminal arm lie within the minor groove of DNA to form direct interactions with bases, whereas the extended conserved region of the C-terminus of the homeodomain interacts with Al to stabilize and localize the third a helix of the Cll homeodomain. This structure suggests a novel mode for the cooperativity of homeodomain proteins. The EMBO Journal (2010) 29, 1613-1623. doi:10.1038/emboj.2010.53; Published online 13 April 2010