Biochemistry (Moscow)

, Volume 80, Issue 8, pp 1047–1056 | Cite as

Molecular dynamics investigation of a mechanism of allosteric signal transmission in ribosomes

  • G. I. Makarov
  • A. V. Golovin
  • N. V. Sumbatyan
  • A. A. Bogdanov


The ribosome is a molecular machine that synthesizes all cellular proteins via translation of genetic information encoded in polynucleotide chain of messenger RNA. Transition between different stages of the ribosome working cycle is strictly coordinated by changes in structure and mutual position both of subunits of the ribosome and its ligands. Therein, information regarding structural transformations is transmitted between functional centers of the ribosome through specific signals. Usually, functional centers of ribosomes are located at a distance reaching up to several tens of angstroms, and it is believed that such signals are transduced allosterically. In our study, we attempted to answer the question of how allosteric signal can be transmitted from one of the so-called sensory elements of ribosomal tunnel (RT) to the peptidyl transferase center (PTC). A segment of RT wall from the E. coli ribosome composed of nucleotide residues A2058, A2059, m2A2503, G2061, A2062, and C2063 of its 23S rRNA was examined by molecular dynamics simulations. It was found that a potential signal transduction pathway A2058-C2063 acted as a dynamic ensemble of interdependent conformational states, wherein cascade-like changes can occur. It was assumed that structural rearrangement in the A2058-C2063 RT segment results in reversible inactivation of PTC due to a strong stacking contact between functionally important U2585 residue of the PTC and nucleotide residue C2063. A potential role for the observed conformational transition in the A2058-C2063 segment for regulating ribosome activity is discussed.

Key words

ribosome ribosomal tunnel allostery molecular dynamics simulations 


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Copyright information

© Pleiades Publishing, Ltd. 2015

Authors and Affiliations

  • G. I. Makarov
    • 1
  • A. V. Golovin
    • 2
  • N. V. Sumbatyan
    • 1
  • A. A. Bogdanov
    • 1
    • 3
  1. 1.Lomonosov Moscow State UniversityFaculty of ChemistryMoscowRussia
  2. 2.Lomonosov Moscow State UniversityFaculty of Bioengineering and BioinformaticsMoscowRussia
  3. 3.Belozersky Institute of Physical-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia

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