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首页> 外文期刊>RNA >RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region.
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RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region.

机译：RNase E通过非催化区域内的蓝细菌特异性九肽与蓝细菌中的多核苷酸磷酸化酶形成复合物。

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摘要

RNase E, a central component involved in bacterial RNA metabolism, usually has a highly conserved N-terminal catalytic domain but an extremely divergent C-terminal domain. While the C-terminal domain of RNase E in Escherichia coli recruits other components to form an RNA degradation complex, it is unknown if a similar function can be found for RNase E in other organisms due to the divergent feature of this domain. Here, we provide evidence showing that RNase E forms a complex with another essential ribonuclease-the polynucleotide phosphorylase (PNPase)-in cyanobacteria, a group of ecologically important and phylogenetically ancient organisms. Sequence alignment for all cyanobacterial RNase E proteins revealed several conserved and variable subregions in their noncatalytic domains. One such subregion, an extremely conserved nonapeptide (RRRRRRSSA) located near the very end of RNase E, serves as the PNPase recognition site in both the filamentous cyanobacterium Anabaena PCC7120 and the unicellular cyanobacterium Synechocystis PCC6803. These results indicate that RNase E and PNPase form a ribonuclease complex via a common mechanism in cyanobacteria. The PNPase-recognition motif in cyanobacterial RNase E is distinct from those previously identified in Proteobacteria, implying a mechanism of coevolution for PNPase and RNase E in different organisms.
机译：RNase E是细菌RNA代谢的重要组成部分，通常具有高度保守的N末端催化结构域，但具有极为不同的C末端结构域。尽管大肠杆菌中RNase E的C末端结构域募集了其他成分以形成RNA降解复合物，但由于该结构域的差异性，在其他生物中是否可以为RNase E找到类似的功能尚不得而知。在这里，我们提供的证据表明，在蓝细菌中，核糖核酸酶E与另一种必不可少的核糖核酸酶-多核苷酸磷酸化酶（PNPase）-形成了复合物。所有蓝藻RNase E蛋白的序列比对揭示了其非催化结构域中的几个保守和可变子区域。一个这样的子区域，一个位于RNase E末端附近的极其保守的九肽（RRRRRRSSA），在丝状蓝细菌Anabaena PCC7120和单细胞蓝细菌Synechocystcystis PCC6803中均充当PNPase识别位点。这些结果表明，RNase E和PNPase通过蓝细菌中的共同机制形成核糖核酸酶复合物。蓝细菌RNase E中的PNPase识别基序与以前在变形杆菌中鉴定出的基序不同，这暗示着PNPase和RNase E在不同生物体中共同进化的机制。

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