Ribosomal protein L27 is a feature of the bacterial ribosome. Based on structural studies, the extended N- terminal tail of protein L27 is known to reach the peptidyl transferase center of the ribosome, where it forms the extensive contacts with helixes H80-H81 of the 23S rRNA as well as several contacts with tRNAs at the A- and P-sites. Shortening of the Escherichia coli protein L27 from N-terminus led to the decrease of the functional activity of the ribosomes. It is supposed that protein L27 plays an important role in the positioning of tRNA in two tRNA-binding sites of the ribosome. In the present work, the role of the contacts of the N-terminal region of protein L27 with the 23S rRNA in the function of the ribosome has been investigated. For this purpose, a number of E. coli strains have been constructed containing protein L27 with the point replacements. It has turned out that some replacements (K4L or K4A/K5G) introduced into the protein lead to the significant slowdown of the cell growth and the decrease in the activity of their translation apparatus. Based on the available structural data, within the ribosome these conservative amino acid residues of protein L27 form the contacts only with 23S rRNA but not with tRNA. The data obtained in the work indicate the importance of the contacts of N-terminal region of protein L27 with the 23S rRNA for the formation of the functionally active bacterial ribosome in vivo .
Escherichia coli, ribosomal protein L27, ribosomal RNA, ribosome, translation, Escherichia coli
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