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Visualization of release factor 3 on the ribosome during termination of protein synthesis

Author

Listed:
  • Bruno P. Klaholz

    (Imperial College London
    Institute of Genetics and Molecular and Cellular Biology, CNRS/INSERM/ULP)

  • Alexander G. Myasnikov

    (Belozersky Institute, Building A, Moscow State University)

  • Marin van Heel

    (Imperial College London)

Abstract

Termination of protein synthesis by the ribosome requires two release factor (RF) classes. The class II RF3 is a GTPase that removes class I RFs (RF1 or RF2) from the ribosome after release of the nascent polypeptide1,2,3. RF3 in the GDP state binds to the ribosomal class I RF complex, followed by an exchange of GDP for GTP and release of the class I RF. As GTP hydrolysis triggers release of RF3 (ref. 4), we trapped RF3 on Escherichia coli ribosomes using a nonhydrolysable GTP analogue. Here we show by cryo-electron microscopy that the complex can adopt two different conformational states. In ‘state 1’, RF3 is pre-bound to the ribosome, whereas in ‘state 2’ RF3 contacts the ribosome GTPase centre. The transfer RNA molecule translocates from the peptidyl site in state 1 to the exit site in state 2. This translocation is associated with a large conformational rearrangement of the ribosome. Because state 1 seems able to accommodate simultaneously both RF3 and RF2, whose position is known from previous studies5,6, we can infer the release mechanism of class I RFs.

Suggested Citation

  • Bruno P. Klaholz & Alexander G. Myasnikov & Marin van Heel, 2004. "Visualization of release factor 3 on the ribosome during termination of protein synthesis," Nature, Nature, vol. 427(6977), pages 862-865, February.
    • Handle: RePEc:nat:nature:v:427:y:2004:i:6977:d:10.1038_nature02332
    DOI: 10.1038/nature02332
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    Cited by:

    1. Asuteka Nagao & Yui Nakanishi & Yutaro Yamaguchi & Yoshifumi Mishina & Minami Karoji & Takafumi Toya & Tomoya Fujita & Shintaro Iwasaki & Kenjyo Miyauchi & Yuriko Sakaguchi & Tsutomu Suzuki, 2023. "Quality control of protein synthesis in the early elongation stage," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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