Biochemistry (Moscow)

, Volume 79, Issue 8, pp 826–835 | Cite as

Mutant forms of Escherichia coli protein L25 unable to bind to 5S rRNA are incorporated efficiently into the ribosome in vivo

  • A. Y. Anikaev
  • A. P. Korepanov
  • A. V. Korobeinikova
  • V. G. Kljashtorny
  • W. Piendl
  • S. V. Nikonov
  • M. B. Garber
  • G. M. GongadzeEmail author


5S rRNA-binding ribosomal proteins of the L25 family are an evolutional acquisition of bacteria. Earlier we showed that (i) single replacements in the RNA-binding module of the protein of this family result in destabilization or complete impossibility to form a complex with 5S rRNA in vitro; (ii) ΔL25 ribosomes of Escherichia coli are less efficient in protein synthesis in vivo than the control ribosomes. In the present work, the efficiency of incorporation of the E. coli protein L25 with mutations in the 5S rRNA-binding region into the ribosome in vivo was studied. It was found that the mutations in L25 that abolish its ability to form the complex with free 5S rRNA do not prevent its correct and efficient incorporation into the ribosome. This is supported by the fact that even the presence of a very weakly retained mutant form of the protein in the ribosome has a positive effect on the activity of the translational machinery in vivo. All this suggests the existence of an alternative incorporation pathway for this protein into the ribosome, excluding the preliminary formation of the complex with 5S rRNA. At the same time, the stable L25-5S rRNA contact is important for the retention of the protein within the ribosome, and the conservative amino acid residues of the RNA-binding module play a key role in this.

Key words

5S rRNA-binding protein L25 RNA-protein interactions ribosome translation Escherichia coli 


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Copyright information

© Pleiades Publishing, Ltd. 2014

Authors and Affiliations

  • A. Y. Anikaev
    • 1
  • A. P. Korepanov
    • 1
  • A. V. Korobeinikova
    • 1
  • V. G. Kljashtorny
    • 1
  • W. Piendl
    • 2
  • S. V. Nikonov
    • 1
  • M. B. Garber
    • 1
  • G. M. Gongadze
    • 1
    Email author
  1. 1.Institute of Protein ResearchRussian Academy of SciencesPushchino, Moscow RegionRussia
  2. 2.Division of Medical Biochemistry, BiocenterInnsbruck Medical UniversityInnsbruckAustria

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