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Structure of the 30S translation initiation complex

Author

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  • Angelita Simonetti

    (Institute of Genetics and of Molecular and Cellular Biology
    Inserm, U596, Illkirch F-67404, France
    CNRS, UMR7104, Illkirch F-67404, France
    Université Louis Pasteur)

  • Stefano Marzi

    (Institute of Genetics and of Molecular and Cellular Biology
    Inserm, U596, Illkirch F-67404, France
    CNRS, UMR7104, Illkirch F-67404, France
    Université Louis Pasteur)

  • Alexander G. Myasnikov

    (Institute of Genetics and of Molecular and Cellular Biology
    Inserm, U596, Illkirch F-67404, France
    CNRS, UMR7104, Illkirch F-67404, France
    Université Louis Pasteur)

  • Attilio Fabbretti

    (Laboratory of Genetics, University of Camerino)

  • Marat Yusupov

    (Institute of Genetics and of Molecular and Cellular Biology
    Inserm, U596, Illkirch F-67404, France
    CNRS, UMR7104, Illkirch F-67404, France
    Université Louis Pasteur)

  • Claudio O. Gualerzi

    (Laboratory of Genetics, University of Camerino)

  • Bruno P. Klaholz

    (Institute of Genetics and of Molecular and Cellular Biology
    Inserm, U596, Illkirch F-67404, France
    CNRS, UMR7104, Illkirch F-67404, France
    Université Louis Pasteur)

Abstract

Protein synthesis: the 30S complex Proteins known as initiation factors (IFs) help to position the 30S subunit of the ribosome correctly on the mRNA start site so that the proper reading frame is engaged. After formation of this 30S initiation complex, the 50S ribosomal subunit binds and the IFs are released. In this work, Simonetti et al. use cryo-electron microscopy to examine the position of the mRNA, initiator tRNA, IF1 and IF2 in the 30S particle. From this structure, they predict how the 50S subunit interacts with the 30S initiation complex, and how GTP bound to IF2 is positioned towards the incoming GTPase-activated centre of the 50S.

Suggested Citation

  • Angelita Simonetti & Stefano Marzi & Alexander G. Myasnikov & Attilio Fabbretti & Marat Yusupov & Claudio O. Gualerzi & Bruno P. Klaholz, 2008. "Structure of the 30S translation initiation complex," Nature, Nature, vol. 455(7211), pages 416-420, September.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7211:d:10.1038_nature07192
    DOI: 10.1038/nature07192
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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.
    2. Alla D. Fedorova & Stephen J. Kiniry & Dmitry E. Andreev & Jonathan M. Mudge & Pavel V. Baranov, 2022. "Thousands of human non-AUG extended proteoforms lack evidence of evolutionary selection among mammals," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Ritwika S. Basu & Michael B. Sherman & Matthieu G. Gagnon, 2022. "Compact IF2 allows initiator tRNA accommodation into the P site and gates the ribosome to elongation," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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