Ribosome biogenesis is an energetically expensive and complex cellular process that involves the coordinated folding of the ribosomal RNA and dozens of ribosomal proteins. It proceeds along multiple parallel pathways and is guided by trans-acting factors called ribosome assembly factors. Although this process has been studied for decades, there are still many open questions regarding the role of the ribosome assembly factors in directing the folding of ribosome biogenesis intermediates. RimP is one of the early acting factors and guides the assembly of the small 30S ribosomal subunit by facilitating the binding of ribosomal proteins uS5 and uS12. Here we report the virtually complete ¹H, ¹⁵N, and ¹³C chemical shift assignment of RimP from Escherichia coli. The NMR chemical shift data, deposited in the BMRB data bank under Accession No. 28014, indicates a widely folded protein composed of three alpha helices and eight beta strands.

中文翻译：

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来自大肠杆菌的核糖体成熟因子 RimP 的主链和侧链 NMR 分配。

核糖体生物发生是一个能量消耗巨大且复杂的细胞过程，涉及核糖体 RNA 和数十种核糖体蛋白的协调折叠。它沿着多个平行途径前进，并由称为核糖体组装因子的反式作用因子引导。尽管这一过程已经研究了几十年，但关于核糖体组装因子在指导核糖体生物发生中间体折叠方面的作用仍然存在许多悬而未决的问题。RimP 是早期作用因子之一，通过促进核糖体蛋白 uS5 和 uS12 的结合来指导 30S 小核糖体亚基的组装。在这里，我们报告了RimP的几乎完整的¹ H、¹⁵ N 和¹³ C 化学位移分配，来自大肠杆菌。NMR 化学位移数据以登录号 28014 存放在 BMRB 数据库中，表明一种广泛折叠的蛋白质，由三个α螺旋和八个β链组成。