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
中科院分区:
文献类型:
--
作者:
METZENBERG, S;JOBLET, C;AGABIAN, N
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.