Function of heterologous and truncated RNase P proteins in Bacillus subtilis
Function of heterologous and truncated RNase P proteins in Bacillus subtilis
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DOI：
10.1111/j.1365-2958.2007.05962.x
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发表时间：
2007-11-01
影响因子：
3.6
通讯作者：
Hartmann, Roland K.
中科院分区：
文献类型：
--
作者：
Goessringer, Markus;Hartmann, Roland K.
细菌RNase P由一个RNA亚基和一个蛋白质（分别由rnpB和rnpA基因编码）组成。枯草芽孢杆菌rnpA敲低菌株V用于筛选来自细菌亚门的代表性谱的细菌RNase P蛋白之间的功能保守性。我们证明了细菌RNase P（RnpA）蛋白的保守功能，尽管低序列保守性。甚至来自嗜冷和嗜热细菌的rnpA基因也挽救了B的生长。枯草d 7菌;同样，在所谓的金属结合环中，β链2和3之间的末端延伸和插入与B中的RnpA功能相容。枯草杆菌。B的缺失分析。枯草杆菌RnpA定义了体内细菌RNase P功能所必需的结构元件。我们进一步扩展了我们在B中的互补分析。枯草杆菌菌株d 7与来自三种不同酵母的四种单独的RNase P蛋白亚基以及作为真核RNase P代表的人Rpp 21和Rpp 29的关系。这些非细菌RNase P蛋白均未显示出能够替代B的任何证据。枯草杆菌RNase P蛋白在体内，支持的概念，古/真核RNase P蛋白是进化无关的细菌RnpA蛋白。
Bacterial RNase P is composed of an RNA subunit and a single protein (encoded by the rnpB and rnpA genes respectively). The Bacillus subtilis rnpA knockdown strain V was used to screen for functional conservation among bacterial RNase P proteins from a representative spectrum of bacterial subphyla. We demonstrate conserved function of bacterial RNase P (RnpA) proteins despite low sequence conservation. Even rnpA genes from psychrophilic and thermophilic bacteria rescued growth of B. subtilis d7 bacteria; likewise, terminal extensions and insertions between beta strands 2 and 3, in the so-called metal binding loop, were compatible with RnpA function in B. subtilis. A deletion analysis of B. subtilis RnpA defined the structural elements essential for bacterial RNase P function in vivo. We further extended our complementation analysis in B. subtilis strain d7 to the four individual RNase P protein subunits from three different Archaea, as well as to human Rpp21 and Rpp29 as representatives of eukaryal RNase P. None of these non-bacterial RNase P proteins showed any evidence of being able to replace the B. subtilis RNase P protein in vivo, supporting the notion that archaeal/eukaryal RNase P proteins are evolutionary unrelated to the bacterial RnpA protein.