Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia.
Nucleic Acids Res. 2012 Oct;40(18):9153-9. doi: 10.1093/nar/gks676. Epub 2012 Jul 20.
In the present work, ribosomes assembled in bacterial cells in the absence of essential ribosomal protein L5 were obtained. After arresting L5 synthesis, Escherichia coli cells divide a limited number of times. During this time, accumulation of defective large ribosomal subunits occurs. These 45S particles lack most of the central protuberance (CP) components (5S rRNA and proteins L5, L16, L18, L25, L27, L31, L33 and L35) and are not able to associate with the small ribosomal subunit. At the same time, 5S rRNA is found in the cytoplasm in complex with ribosomal proteins L18 and L25 at quantities equal to the amount of ribosomes. Thus, it is the first demonstration that protein L5 plays a key role in formation of the CP during assembly of the large ribosomal subunit in the bacterial cell. A possible model for the CP assembly in vivo is discussed in view of the data obtained.
在本工作中，获得了在缺乏必需核糖体蛋白 L5 的情况下在细菌细胞中组装的核糖体。在抑制 L5 合成后，大肠杆菌细胞分裂有限次数。在此期间，会积累有缺陷的大亚基核糖体。这些 45S 颗粒缺少大部分中央突出（CP）成分（5S rRNA 和蛋白质 L5、L16、L18、L25、L27、L31、L33 和 L35），并且无法与小核糖体亚基结合。同时，5S rRNA 在细胞质中与核糖体蛋白 L18 和 L25 以等于核糖体数量的量复合存在。因此，这首次证明了在细菌细胞中大核糖体亚基组装过程中，蛋白质 L5 在 CP 的形成中起关键作用。根据获得的数据，讨论了 CP 组装的可能模型。
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