Biochemistry (Moscow)

, Volume 69, Issue 12, pp 1319-1323

First online:

Role of N-terminal helix in interaction of ribosomal protein S15 with 16S rRNA

  • S. V. RevtovichAffiliated withInstitute of Protein Research, Russian Academy of Sciences
  • , A. D. NikulinAffiliated withInstitute of Protein Research, Russian Academy of Sciences Email author 
  • , S. V. NikonovAffiliated withInstitute of Protein Research, Russian Academy of Sciences

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The position and conformation of the N-terminal helix of free ribosomal protein S15 was earlier found to be modified under various conditions. This variability was supposed to provide the recognition by the protein of its specific site on 16S rRNA. To test this hypothesis, we substituted some amino acid residues in this helix and assessed effects of these substitutions on the affinity of the protein for 16S rRNA. The crystal structure of the complex of one of these mutants (Thr3Cys S15) with the 16S rRNA fragment was determined, and a computer model of the complex containing another mutant (Gln8Met S15) was designed. The available and new information was analyzed in detail, and the N-terminal helix was concluded to play no significant role in the specific binding of the S15 protein to its target on 16S rRNA.

Key words

RNA-protein interactions ribosomal proteins crystal structure S15 protein 16S ribosomal RNA