Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
Biochemistry (Mosc). 2012 Jun;77(6):562-74. doi: 10.1134/S0006297912060028.
The question concerning reasons for the variety of ribosomal proteins that arose for more than 40 years ago is still open. Ribosomes of modern organisms contain 50-80 individual proteins. Some are characteristic for all domains of life (universal ribosomal proteins), whereas others are specific for bacteria, archaea, or eucaryotes. Extensive information about ribosomal proteins has been obtained since that time. However, the role of the majority of ribosomal proteins in the formation and functioning of the ribosome is still not so clear. Based on recent data of experiments and bioinformatics, this review presents a comprehensive evaluation of structural conservatism of ribosomal proteins from evolutionarily distant organisms. Considering the current knowledge about features of the structural organization of the universal proteins and their intermolecular contacts, a possible role of individual proteins and their structural elements in the formation and functioning of ribosomes is discussed. The structural and functional conservatism of the majority of proteins of this group suggests that they should be present in the ribosome already in the early stages of its evolution.
核糖体蛋白多样性的原因这一问题早在 40 多年前就出现了,但至今仍未得到解决。现代生物的核糖体包含 50-80 种不同的蛋白质。有些蛋白质是所有生命领域所共有的(通用核糖体蛋白),而另一些则是细菌、古菌或真核生物所特有的。自那时以来,人们已经获得了大量关于核糖体蛋白的信息。然而,大多数核糖体蛋白在核糖体的形成和功能中的作用仍然不是很清楚。基于最近的实验和生物信息学数据,本文对进化上不同的生物体的核糖体蛋白的结构保守性进行了全面评估。考虑到目前关于通用蛋白的结构组织特征及其分子间相互作用的知识,本文讨论了个别蛋白质及其结构元件在核糖体的形成和功能中的可能作用。该组大多数蛋白质的结构和功能保守性表明,它们应该在核糖体的早期进化阶段就已经存在了。