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Related Experiment Videos

Structure and function of the acidic ribosomal stalk proteins.

Markus C Wahl1, Wim Möller

  • 1Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany. mwahl@biochem.mpg.de

Current Protein & Peptide Science
|October 9, 2002
PubMed
Summary

Acidic ribosomal proteins L7/L12 and P1/P2 act as GTPase activating proteins, crucial for translation factor function and GTP hydrolysis during protein synthesis. Their structure and function are conserved across species, despite sequence diversity.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Acidic ribosomal proteins L7/L12 (prokaryotes) and P1/P2 (eukaryotes) are unique, multi-copy components of the ribosome's stalk protuberance.
  • These proteins do not directly bind ribosomal RNA but interact via other ribosomal proteins (L10 and P0, respectively).
  • They are known to be involved in translation factor binding and stimulating GTP hydrolysis.

Purpose of the Study:

  • To elucidate the role of acidic ribosomal proteins in GTPase activation and translation.
  • To investigate the structural organization and functional conservation of these proteins.
  • To understand the mechanism of GTPase activation and the role of ribosomal environment.

Main Methods:

  • In vitro studies using isolated ribosomal proteins and components.

Related Experiment Videos

  • Analysis of GTP-hydrolysis stimulation by L7/L12 and P-proteins.
  • Sequence comparisons and stalk transplantation experiments.
  • Analysis of crystal structures and comparison with physico-chemical data.

    • Main Results:

    • L7/L12 proteins function as GTPase activating proteins (GAPs) for elongation factors (EF-Tu and EF-G).
    • The ribosome-dependent GTP hydrolysis stimulated by L7/L12 is maximal with four copies and reflects in vivo rates.
    • Structural studies reveal conserved functional domains (N-terminal for oligomerization, C-terminal for factor interaction, hinge for flexibility) and diverse quaternary structures.
    • Stalk transplantation experiments suggest coevolution of stalk proteins and factors (EF-G, EF-2).

    Conclusions:

    • Acidic ribosomal proteins L7/L12/P1/P2 are essential GAPs, acting as a 'landing platform' for translation factors to induce GTP hydrolysis.
    • Their function is modulated by the ribosomal environment, particularly sensing codon-anticodon pairing for EF-Tu.
    • Despite sequence diversity, conserved functional domains and genetic organization highlight coevolutionary adaptations for maintaining ribosome function across species.