RsgA与核糖体之间的相互作用。

Interaction between RsgA and the ribosome.

作者信息

Kimura Takatsugu, Takagi Kuniaki, Kyoko Hanawa-Suetsugu, Kalachnyuk Liliya, Muto Akira, Himeno Hyouta

机构信息

Department of Biochemistry and Biotechnology, Faculty of Agriculture and Life Science, Hirosaki University.

出版信息

Nucleic Acids Symp Ser (Oxf). 2007(51):375-6. doi: 10.1093/nass/nrm188.

DOI:10.1093/nass/nrm188

PMID:18029743

Abstract

RsgA is a unique GTP hydrolytic protein that is widely found in bacteria and plants, and is activated by the small subunit of the ribosome. Disruption of the gene for RsgA from the genome affects the growth of cells, the subunit association of the ribosome in cells and maturation of 16S ribosomal RNA. Here, we investigated the interaction between EscherichiacoliRsgA and the ribosome. Several antibiotics bound to the decoding center of the small subunit inhibited the ribosome-dependent GTPase activity of RsgA, suggesting that RsgA binds to the decoding center. Chemical footprinting was also performed to further investigate the interaction.

摘要

RsgA是一种独特的GTP水解蛋白，广泛存在于细菌和植物中，并由核糖体小亚基激活。从基因组中破坏RsgA基因会影响细胞生长、细胞中核糖体的亚基缔合以及16S核糖体RNA的成熟。在这里，我们研究了大肠杆菌RsgA与核糖体之间的相互作用。几种与小亚基解码中心结合的抗生素抑制了RsgA的核糖体依赖性GTP酶活性，这表明RsgA与解码中心结合。还进行了化学足迹分析以进一步研究这种相互作用。