COMMON AND SPECIFIC STRUCTURAL FEATURES OF THE RIBOSOMAL-PROTEIN L1 FROM BACTERIA AND ARCHAEA

Detailed analysis of the spatial structure of the ribosomal protein L1 from Thermus thermophilus revealed structurally important amino acid residues. Comparison of known L1 sequences from ten Bacteria and six A rchaea showed that all key residues are either identical or conserved. Thereby, conservation of the spatial structure of L1 proteins is sugg ested. Some structural differences between bacterial and archaeal L1 p roteins are proposed, basing on lower sequence homology between these two groups of organisms as compared with that within each group and on the structural role of homologous regions.