A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.
A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.
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DOI：
10.1016/j.str.2016.04.001
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发表时间：
2016-06-07
期刊：
影响因子：
--
通讯作者：
Pelicic V
中科院分区：
文献类型：
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作者：
Berry JL;Xu Y;Ward PN;Lea SM;Matthews SJ;Pelicic V
DNA转化是一种广泛的过程，允许细菌通过使用由IV型菌毛蛋白组成的丝状纳米机器捕获游离DNA。这些蛋白质可以作为DNA受体，如脑膜炎奈瑟氏球菌ComP次要菌毛蛋白具有内在DNA结合能力的发现所证明的。当ComP含有在该物种基因组中丰富的DNA摄取序列（DUS）基序时，ComP更好地结合DNA，在其选择性摄取自身DNA的商标能力中发挥作用。在这里，我们报告了脑膜炎球菌ComP和金黄色奈瑟菌ComPsub的高分辨率结构，它们识别不同的DUS基序。我们发现，它们是结构相同的IV型菌毛蛋白，包装容易成细丝模型，并显示一个独特的DD区域由两个二硫键界定。ComPsub的功能分析定义了一种新的DNA结合模式，涉及DD区域，适用于输出的DNA受体。ComP直系同源物是IV型菌毛蛋白结合DNA，自然转化的关键两个高分辨率结构揭示了一个独特的菌毛蛋白折叠DNA结合涉及一个新的基序ComP是第一个具有DNA结合能力的IV型菌毛蛋白，在奈瑟氏球菌科的自然转化的关键。通过报道两个ComP直系同源物的高分辨率结构，Berry et al.揭示了DNA结合的新模式
DNA transformation is a widespread process allowing bacteria to capture free DNA by using filamentous nano-machines composed of type IV pilins. These proteins can act as DNA receptors as demonstrated by the finding that Neisseria meningitidis ComP minor pilin has intrinsic DNA-binding ability. ComP binds DNA better when it contains the DNA-uptake sequence (DUS) motif abundant in this species genome, playing a role in its trademark ability to selectively take up its own DNA. Here, we report high-resolution structures for meningococcal ComP and Neisseria subflava ComPsub, which recognize different DUS motifs. We show that they are structurally identical type IV pilins that pack readily into filament models and display a unique DD region delimited by two disulfide bonds. Functional analysis of ComPsub defines a new mode of DNA binding involving the DD region, adapted for exported DNA receptors. ComP orthologs are type IV pilins binding DNA, key for natural transformation Two high-resolution structures reveal a unique pilin fold DNA binding involves a novel motif ComP is the first type IV pilin with DNA-binding ability, key for natural transformation in Neisseriaceae. By reporting high-resolution structures for two ComP orthologs, Berry et al. shed light on a novel mode of DNA binding.