RIBOSOMAL PROTEIN-L25 FROM TRYPANOSOMA-BRUCEI - PHYLOGENY AND MOLECULAR COEVOLUTION OF AN RIBOSOMAL-RNA-BINDING PROTEIN AND ITS RIBOSOMAL-RNA BINDING-SITE

RIBOSOMAL PROTEIN-L25 FROM TRYPANOSOMA-BRUCEI - PHYLOGENY AND MOLECULAR COEVOLUTION OF AN RIBOSOMAL-RNA-BINDING PROTEIN AND ITS RIBOSOMAL-RNA BINDING-SITE
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DOI:
10.1093/nar/21.21.4936
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发表时间:
1993-10-25
影响因子:
14.9
通讯作者:
AGABIAN, N
AGABIAN, N
中科院分区:
生物学2区
文献类型:
--
作者:
METZENBERG, S;JOBLET, C;AGABIAN, N

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编码核糖体蛋白L25的基因是从原生动物寄生虫布氏锥虫中分离出的一种主要的rRNA结合蛋白。杂交研究表明,该基因的多个拷贝存在于每个T。布鲁氏菌单倍体基因组。T.布氏杆菌与来自大鼠的L23 a蛋白、来自真菌物种的L25蛋白以及来自真细菌、古细菌和叶绿体的L23蛋白惊人地相似。L23/25蛋白及其各自LSU-rRNA(大亚基rRNA)上的假定结合位点的系统发育分析为研究RNA分子和与其结合的蛋白质之间的分子共进化提供了难得的机会。
The gene encoding ribosomal protein L25, a primary rRNA-binding protein, was isolated from the protozoan parasite Trypanosoma brucei. Hybridization studies indicate that multiple copies of the gene are present per T. brucei haploid genome. The C-terminal domain of L25 protein from T. brucei is strikingly similar to L23a protein from rat, L25 proteins from fungal species, and L23 proteins from eubacteria, archaebacteria, and chloroplasts. A phylogenetic analysis of L23/25 proteins and the putative binding sites on their respective LSU-rRNAs (large subunit rRNAs) provides a rare opportunity to study molecular co-evolution between an RNA molecule and the protein that binds to it.