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

Bruno P. Klaholz (), Alexander G. Myasnikov and Marin van Heel
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Bruno P. Klaholz: Imperial College London
Alexander G. Myasnikov: Belozersky Institute, Building A, Moscow State University
Marin van Heel: Imperial College London

Nature, 2004, vol. 427, issue 6977, 862-865

Abstract: 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.

Date: 2004
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DOI: 10.1038/nature02332

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