Structure of the Escherichia coli ProQ RNA-binding protein.
Structure of the Escherichia coli ProQ RNA-binding protein.
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DOI：
10.1261/rna.060343.116
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发表时间：
2017-05
期刊：
影响因子：
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通讯作者：
Broadhurst RW
中科院分区：
文献类型：
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作者：
Gonzalez GM;Hardwick SW;Maslen SL;Skehel JM;Holmqvist E;Vogel J;Bateman A;Luisi BF;Broadhurst RW
蛋白质ProQ最近已被确定为沙门氏菌中的一个全球性的小的非编码RNA结合蛋白，并且预期其在不同细菌物种中的许多同源物具有类似的作用。我们报告的解决方案结构的大肠杆菌ProQ，揭示了一个N-末端FinO样结构域，C-末端结构域，意想不到的都铎结构域折叠常见于真核生物中，和一个细长的桥接intradomain连接器，是灵活的，但仍然不可压缩。基于结构的序列分析表明，Tudor结构域是通过水平基因转移和基因融合到祖先的FinO样结构域获得的。通过生物化学和生物物理方法的结合，我们已经映射了所有三个领域的ProQ和建模的蛋白质的构象在载脂蛋白和RNA结合的形式推定的RNA结合表面。综上所述，这些数据表明，FinO，Tudor和接头结构域的ProQ合作，以识别复杂的RNA结构，并有助于促进RNA介导的调节。
The protein ProQ has recently been identified as a global small noncoding RNA-binding protein in Salmonella, and a similar role is anticipated for its numerous homologs in divergent bacterial species. We report the solution structure of Escherichia coli ProQ, revealing an N-terminal FinO-like domain, a C-terminal domain that unexpectedly has a Tudor domain fold commonly found in eukaryotes, and an elongated bridging intradomain linker that is flexible but nonetheless incompressible. Structure-based sequence analysis suggests that the Tudor domain was acquired through horizontal gene transfer and gene fusion to the ancestral FinO-like domain. Through a combination of biochemical and biophysical approaches, we have mapped putative RNA-binding surfaces on all three domains of ProQ and modeled the protein's conformation in the apo and RNA-bound forms. Taken together, these data suggest how the FinO, Tudor, and linker domains of ProQ cooperate to recognize complex RNA structures and serve to promote RNA-mediated regulation.