1997
DOI: 10.1007/pl00000578
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Phylogenetic relationship of organisms obtained by ribosomal protein comparison

Abstract: The evolutionary relationships of ribosomal proteins from eubacteria, archaea, eukaryotes, chloroplasts and mitochondria were examined by their degree of conservation, their structural and functional properties and by the occurrence of conserved structural elements. The structural domains formed by the different protein families were studied. The occurrence of monophyletic groups was investigated for each protein family within the archaea. Phylogenetic trees were constructed between these organisms and togethe… Show more

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Cited by 31 publications
(20 citation statements)
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“…Ribosomal protein L6 is one of the most highly conserved ribosomal proteins located at the factor binding site of the large subunit (15,22). The SERF technique identified a consensus sequence U2739-C2789 of domain VI of 23S as the binding site of L6 after four rounds of selection (blue in Fig.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Ribosomal protein L6 is one of the most highly conserved ribosomal proteins located at the factor binding site of the large subunit (15,22). The SERF technique identified a consensus sequence U2739-C2789 of domain VI of 23S as the binding site of L6 after four rounds of selection (blue in Fig.…”
Section: Resultsmentioning
confidence: 99%
“…L4 is essential for early events of the 50S assembly (20) and seems to be adjacent to the peptidyl-transferase center (21). L6 is one of the most conserved proteins and is present in ribosomes of all organisms (22) at or near the elongation-factor binding site (15). Furthermore, preliminary experiments demonstrated a low unspecific binding of these proteins to an rRNA fragment pool.…”
mentioning
confidence: 99%
“…In general, structural proteins such as tubulin, actin, and ribosomal proteins show high levels of sequence conservation (15,26,38). In fact, functionality within the Cbf5p-NAP57 family is conserved between widely divergent species; e.g., the Drosophila CBF5 homolog cDNA complements the cbf5⌬ null allele when introduced into yeast on a plasmid and expressed under the control of the yeast ADH1 promoter (8).…”
Section: Discussionmentioning
confidence: 99%
“…Although protein L2 is among the most conserved ribosomal proteins throughout evolution [9,27], the proteins used in our experiments are rather divergent when compared with their E. coli counterpart. Protein L2 from the halophilic archaebacterium H. marismortui (HmaL2) shows 36 % identical amino acids in comparison with the eubacterial L2 protein, and the human equivalent (HumanL8) only 30 % identity with its E. coli homologue.…”
Section: Discussionmentioning
confidence: 99%