Crystal structures of CDC21-1 inteins from hyperthermophilic archaea reveal the selection mechanism for the highly conserved homing endonuclease insertion site
Crystal structures of CDC21-1 inteins from hyperthermophilic archaea reveal the selection mechanism for the highly conserved homing endonuclease insertion site
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DOI：
10.1007/s00792-019-01117-4
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发表时间：
2019-11-01
期刊：
影响因子：
2.9
通讯作者：
Iwai, Hideo
中科院分区：
文献类型：
--
作者：
Beyer, Hannes M.;Mikula, Kornelia M.;Iwai, Hideo
自剪接内含子是一种可移动的遗传元件，通过嵌套的归巢内切酶(HEN)结构域入侵宿主基因。位于内含子内的所有HEN结构域都被插入到高度保守的插入位点。指示母鸡插入位置的纯化选择机制尚未确定。在这项工作中，我们解决了插入到嗜热古生菌细胞分裂控制蛋白21中的两个内含子的三维晶体结构。这两种结构的比较为进化过程中丢失HEN结构域的内含子的热稳定机制提供了结构基础。Horikoshii的内含素结构中存在完整的Extein结构域，这表明高度保守的HEN插入点的选择机制。
Self-splicing inteins are mobile genetic elements invading host genes via nested homing endonuclease (HEN) domains. All HEN domains residing within inteins are inserted at a highly conserved insertion site. A purifying selection mechanism directing the location of the HEN insertion site has not yet been identified. In this work, we solved the three-dimensional crystal structures of two inteins inserted in the cell division control protein 21 of the hyperthermophilic archaea Pyrococcus abyssi and Pyrococcus horikoshii. A comparison between the structures provides the structural basis for the thermo-stabilization mechanism of inteins that have lost the HEN domain during evolution. The presence of an entire extein domain in the intein structure from Pyrococcus horikoshii suggests the selection mechanism for the highly conserved HEN insertion point.