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A cryo-electron microscopic study of ribosome-bound termination factor RF2

Author

Listed:
  • Urmila B. S. Rawat

    (Howard Hughes Medical Institute, Health Research, Inc.
    Wadsworth Center)

  • Andrey V. Zavialov

    (Uppsala University)

  • Jayati Sengupta

    (Wadsworth Center)

  • Mikel Valle

    (Howard Hughes Medical Institute, Health Research, Inc.
    Wadsworth Center)

  • Robert A. Grassucci

    (Howard Hughes Medical Institute, Health Research, Inc.
    Wadsworth Center)

  • Jamie Linde

    (Wadsworth Center)

  • Bente Vestergaard

    (University of Aarhus)

  • Måns Ehrenberg

    (Uppsala University)

  • Joachim Frank

    (Howard Hughes Medical Institute, Health Research, Inc.
    Wadsworth Center
    State University of New York at Albany)

Abstract

Protein synthesis takes place on the ribosome, where genetic information carried by messenger RNA is translated into a sequence of amino acids. This process is terminated when a stop codon moves into the ribosomal decoding centre (DC) and is recognized by a class-1 release factor (RF). RFs have a conserved GGQ amino-acid motif, which is crucial for peptide release and is believed to interact directly with the peptidyl-transferase centre (PTC) of the 50S ribosomal subunit1,2. Another conserved motif of RFs (SPF in RF2) has been proposed to interact directly with stop codons in the DC of the 30S subunit3. The distance between the DC and PTC is ∼73 Å. However, in the X-ray structure of RF2, SPF and GGQ are only 23 Å apart4, indicating that they cannot be at DC and PTC simultaneously. Here we show that RF2 is in an open conformation when bound to the ribosome, allowing GGQ to reach the PTC while still allowing SPF–stop-codon interaction. The results indicate new interpretations of accuracy in termination, and have implications for how the presence of a stop codon in the DC is signalled to PTC.

Suggested Citation

  • Urmila B. S. Rawat & Andrey V. Zavialov & Jayati Sengupta & Mikel Valle & Robert A. Grassucci & Jamie Linde & Bente Vestergaard & Måns Ehrenberg & Joachim Frank, 2003. "A cryo-electron microscopic study of ribosome-bound termination factor RF2," Nature, Nature, vol. 421(6918), pages 87-90, January.
    • Handle: RePEc:nat:nature:v:421:y:2003:i:6918:d:10.1038_nature01224
    DOI: 10.1038/nature01224
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    Cited by:

    1. Aymen S Yassin & Rajendra K Agrawal & Nilesh K Banavali, 2011. "Computational Exploration of Structural Hypotheses for an Additional Sequence in a Mammalian Mitochondrial Protein," PLOS ONE, Public Library of Science, vol. 6(7), pages 1-10, July.

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