Solution structure of TA1092, a ribosomal protein S24e from Thermoplasma acidophilum
Solution structure of TA1092, a ribosomal protein S24e from Thermoplasma acidophilum
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DOI:
10.1002/prot.21045
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发表时间:
2006-09-01
影响因子:
2.9
通讯作者:
Lee, Weontae
中科院分区:
文献类型:
--
作者:
Jeon, Byoung-Young;Jung, Jinwon;Lee, Weontae
Introduction. The ribosome is a large ribonucleoprotein complex that catalyzes protein synthesis. In archaea, the ribosome is composed of a small 30S subunit and a large 50S subunit. The 30S subunit of the archaea ribosome is composed of a 16S rRNA and 28 ribosomal proteins. Genes that encode ribosomal proteins consist of multiple processed pseudogenes, which are dispersed through the genome. Recent advances in ribosome structure1 suggest close molecular interactions between rRNA and ribosomal protein, within ribosomal subunits. However, the structural role of ribosomal components during various stages of translation remains to be characterized. Here we report the solution structure of TA1092, a member of the S24e protein family from Thermoplasma acidophilum. 2 Members of the S24e protein family are components of the 30S subunit in both archaea and eukaryotes. Because the detailed structure of ribosomal protein S24e is not yet available for model organisms, the structure of TA1092 will expand our knowledge and understanding of 30S ribosomal protein structure–function for different species.Methods and Materials. The TA1092 gene was cloned into the expression vector, pET15b, and overexpressed in Escherichia coli strain BL21 (DE3)(Novagen Inc., Madison, WI). The cells were grown on a minimal M9 medium, with 15NH4Cl and 13C-glucose to obtain uniformly labeled