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Ribosome recycling depends on mechanistic link between FeS cluster domain and a conformational switch of the twin-ATPase ABCE1

February 2011. Despite all phyla of life show similarities in protein synthesis, the final phase of mRNA translation has yet to be captured. A team of scientists from Frankfurt, Marburg and Rome under the leadership of Robert Tampé has now revealed the ancestral role and mechanistic principles of the newly identified twin-ATPase ABCE1 in ribosome recycling. They demonstrated that the unique iron-sulfur cluster domain and an ATP-dependent conformational switch of ABCE1 are essential both for ribosome binding and recycling. By direct (1:1) interaction, the peptide release factor aRF1 has been shown to synergistically promote ABCE1 function in posttermination ribosome recycling. Upon ATP binding, ABCE1 undergoes a conformational switch from an open to a closed ATP-occluded state, which drives ribosome dissociation as well as the disengagement of aRF1. ATP hydrolysis is not required for a single round of ribosome splitting but for ABCE1 release from the 30S subunit to reenter a new cycle. The results published on 3 February in the Proceedings of the National Academy of Sciences of the USA provide a mechanistic understanding of final phases in mRNA translation.

 

 

Contact
Professor Robert Tampé
Institute of Biochemistry
Goethe University Frankfurt
Frankfurt am Main
Germany
Tel.: +49 (0)69 79829 475/76
Fax: +49 (0)69 798 29495
e-mail: tampe@em.uni-frankfurt.de
www.biochem.uni-frankfurt.de

 

Full paper
Dominik Barthelme, Stephanie Dinkelaker, Sonja-Verena Albers, Paola Londei, Ulrich Ermler, Robert Tampé. 2011. Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1. Proceedings of the National Academy of Sciences USA. Published online before print 3 February 2011, doi: 10.1073/pnas.1015953108