Derivatives of the yeast mitochondrial ribosomal protein MrpS28 replace ribosomal protein S15 as functional components of the Escherichia coli ribosome.

Derivatives of the yeast mitochondrial ribosomal protein MrpS28 replace ribosomal protein S15 as functional components of the Escherichia coli ribosome.
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酵母线粒体核糖体蛋白MrpS28的衍生物取代核糖体蛋白S15作为大肠杆菌核糖体的功能成分。

DOI:
10.1006/jmbi.1993.1539
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发表时间:
1993
影响因子:
5.6
通讯作者:
Ellis,SR
Ellis,SR
中科院分区:
生物学2区
文献类型:
--
作者:
Li,Y;Huff,MO;Hanic-Joyce,PJ;Ellis,SR

文献摘要

被引文献

相似文献

线粒体核糖体蛋白 MrpS28 比其真细菌同源物大肠杆菌核糖体蛋白 S15 (Eco S15) 大得多。相对于跨越细菌蛋白全长的同源区域,成熟的MrpS28在其氨基和羧基末端分别延伸了117和48个氨基酸。 MrpS28 的氨基末端和 S15 样结构域对于酵母线粒体的功能至关重要。在这里,我们展示了这两个相同的结构域在 E 中的功能。大肠杆菌。 MrpS28 的 S15 样结构域单独补充了大肠杆菌中的冷敏感突变。大肠杆菌菌株 KR121 会导致 Eco S15 水平降低。然而,与 Eco S15 相比,MrpS28 的 S15 样结构域的互补效率较低。令人惊讶的是,MrpS28 的氨基末端结构域显然是线粒体核糖体的独特组成部分,本身无法补充冷敏感表型,但却增强了 S15 样结构域支持 KR121 细胞在不允许的温度下生长的能力。总之,这些数据表明氨基末端结构域有助于涉及线粒体和E的组装和功能的MrpS28的基本特性。大肠杆菌糖体。
The mitochondrial ribosomal protein MrpS28 is considerably larger than its eubacterial homolog,Escherichia coliribosomal protein S15 (Eco S15). Relative to a region of homology that spans the entire length of the bacterial protein, mature MrpS28 is extended by 117 and 48 amino acids at its amino and carboxyl termini, respectively. Both the amino-terminal and S15-like domains of MrpS28 are essential for function in yeast mitochondria. Here, we show that these same two domains function inE. coli. The S15-like domain of MrpS28 alone complements a cold sensitive mutation inE. colistrain KR121 that gives rise to reduced levels of Eco S15. However, complementation by the S15-like domain of MrpS28 is inefficient when compared with Eco S15. Surprisingly, the amino-terminal domain of MrpS28, which is apparently a unique component of the mitochondrial ribosome and is unable by itself to complement the cold-sensitive phenotype, enhances the ability of the S15-like domain to support growth of KR121 cells at, nonpermissive temperatures. Together, these data suggest that the amino terminal domain contributes to the fundamental properties of MrpS28 involved in the assembly and function of both mitochondrial andE. coliribosomes.