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Cyanobacteria contain a structural homologue of the Hfq protein with altered RNA-binding properties

机译:蓝细菌包含具有改变的RNA结合特性的Hfq蛋白的结构同源物

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摘要

Hfq proteins are common in many species of enterobacteria, where they participate in RNA folding and translational regulation through pairing of small RNAs and messenger RNAs. Hfq proteins share the distinctive Sm fold, and form ring-shaped structures similar to those of the Sm/Lsm proteins regulating mRNA turnover in eukaryotes. However, bacterial Hfq proteins are homohexameric, whereas eukaryotic Sm/Lsm proteins are heteroheptameric. Recently, Hfq proteins with poor sequence conservation were identified in archaea and cyanobacteria. In this article, we describe crystal structures of the Hfq proteins from the cyanobacteria Synechocystis sp. PCC 6803 and Anabaena PCC 7120 at 1.3 and 2.3 c resolution, respectively, and show that they retain the classic Sm fold despite low sequence conservation. In addition, the intersubunit contacts and RNA-binding site are divergent, and we show biochemically that the proteins bind very weakly to known Escherichia coli Hfq target RNAs in vitro. Moreover, when expressed in E. coli, the proteins cannot mediate Hfq-dependent RNA regulation. It therefore appears that the cyanobacterial proteins constitute a specialized subfamily of Hfq proteins that bind relatively weakly to A/U-rich tracks of regulatory RNAs. The results have implications for our understanding of the evolution of the Sm fold and the Hfq proteins in the bacterial kingdom in general.
机译:Hfq蛋白在许多肠道细菌中很常见,它们通过小RNA和信使RNA的配对参与RNA折叠和翻译调控。 Hfq蛋白具有独特的Sm折叠,并形成类似于Sm / Lsm蛋白质的环状结构,可调节真核生物中的mRNA转换。但是,细菌Hfq蛋白是同六聚体,而真核Sm / Lsm蛋白是异七聚体。最近,在古细菌和蓝细菌中发现了序列保守性差的Hfq蛋白。在本文中,我们描述了蓝藻集胞藻sp。Hfq蛋白的晶体结构。 PCC 6803和Anabaena PCC 7120的分辨率分别为1.3和2.3 c,表明尽管序列保守性低,它们仍保留了经典的Sm折叠。此外,亚基间的接触和RNA结合位点是不同的,并且我们从生化方面证明了蛋白质在体外与已知的大肠杆菌Hfq靶RNA的结合非常弱。此外,当在大肠杆菌中表达时,这些蛋白质不能介导Hfq依赖性RNA调节。因此,似乎蓝细菌蛋白构成了Hfq蛋白的一个特殊的亚家族,它与A / U富集的调节RNA相对较弱地结合。这些结果对于我们对细菌界中Sm折叠和Hfq蛋白的进化的理解具有重要意义。

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