Deryusheva Evgenia I, Machulin Andrey V, Surin Alexey A, Kravchenko Sergey V, Surin Alexey K, Galzitskaya Oxana V
Institute for Biological Instrumentation, Federal Research Center "Pushchino Scientific Center for Biological Research of Russian Academy of Science", Russian Academy of Science, 142290 Pushchino, Russia.
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Federal Research Center "Pushchino Scientific Center for Biological Research of Russian Academy of Science", Russian Academy of Science, 142290 Pushchino, Russia.
Int J Mol Sci. 2024 Dec 4;25(23):13057. doi: 10.3390/ijms252313057.
The RNA-binding S1 domain is a β-barrel with a highly conserved RNA-binding site on its surface. This domain is an important part of the structures of different bacterial, archaeal, and eukaryotic proteins. A distinctive feature of the S1 domain is multiple presences (structural repeats) in proteins and protein complexes. Here, we have analyzed all available protein sequences in the UniProt database to obtain data on the distribution of bacterial, eukaryotic and archaeal proteins containing the S1 domain. Mainly, the S1 domain is found in bacterial proteins with the number of domains varying from one to eight. Eukaryotic proteins contain from one to fifteen S1 domains, while in archaeal proteins, only one S1 domain is identified. Analysis of eukaryotic proteins containing S1 domains revealed a group of chloroplast S1 ribosomal proteins (ChRpS1) with characteristic properties of bacterial S1 ribosomal proteins (RpS1) from the Cyanobacteria. Also, in a separate group, chloroplast and mitochondrial elongation factor Ts containing two S1 structural domains were assigned. For mitochondrial elongation factor Ts, the features of S1 in comparison with the RpS1 from Cyanobacteria phylum and the Alphaproteobacteria class were revealed. The data obtained allow us to consider the S1 domain as one of the evolutionary markers of the symbiogenesis of bacterial and eukaryotic organisms.
RNA 结合 S1 结构域是一个 β 桶状结构，其表面有一个高度保守的 RNA 结合位点。该结构域是不同细菌、古细菌和真核生物蛋白质结构的重要组成部分。S1 结构域的一个显著特征是在蛋白质和蛋白质复合物中多次出现（结构重复）。在这里，我们分析了 UniProt 数据库中所有可用的蛋白质序列，以获取有关含有 S1 结构域的细菌、真核生物和古细菌蛋白质分布的数据。主要发现，S1 结构域存在于细菌蛋白质中，其结构域数量从 1 到 8 不等。真核生物蛋白质含有 1 到 15 个 S1 结构域，而在古细菌蛋白质中，仅鉴定出一个 S1 结构域。对含有 S1 结构域的真核生物蛋白质的分析揭示了一组具有蓝细菌细菌 S1 核糖体蛋白（RpS1）特征性质的叶绿体 S1 核糖体蛋白（ChRpS1）。此外，在一个单独的组中，分配了含有两个 S1 结构域的叶绿体和线粒体延伸因子 Ts。对于线粒体延伸因子 Ts，揭示了其 S1 结构域与蓝细菌门和变形菌纲的 RpS1 相比的特征。所获得的数据使我们能够将 S1 结构域视为细菌和真核生物共生起源的进化标记之一。
