Author
Listed:
- Andreas H. Ratje
(Institut für Medizinische Physik und Biophysik, Charite – Universitätsmedizin Berlin, Ziegelstrasse 5–9, 10117-Berlin, Germany
Institut für Pharmazeutische Chemie, Philipps-Universität Marburg)
- Justus Loerke
(Institut für Medizinische Physik und Biophysik, Charite – Universitätsmedizin Berlin, Ziegelstrasse 5–9, 10117-Berlin, Germany)
- Aleksandra Mikolajka
(Ludwig-Maximilians-Universität, Feodor-Lynenstrasse 25, 81377 München, Germany
Center for Integrated Protein Science, Ludwig-Maximilians-Universität München)
- Matthias Brünner
(Institut für Medizinische Physik und Biophysik, Charite – Universitätsmedizin Berlin, Ziegelstrasse 5–9, 10117-Berlin, Germany)
- Peter W. Hildebrand
(Institut für Medizinische Physik und Biophysik, Charite – Universitätsmedizin Berlin, Ziegelstrasse 5–9, 10117-Berlin, Germany)
- Agata L. Starosta
(Ludwig-Maximilians-Universität, Feodor-Lynenstrasse 25, 81377 München, Germany)
- Alexandra Dönhöfer
(Ludwig-Maximilians-Universität, Feodor-Lynenstrasse 25, 81377 München, Germany)
- Sean R. Connell
(Frankfurt Institute for Molecular Life Sciences, Institute of Organic Chemistry and Chemical Biology, Goethe University Frankfurt, Max-von Laue-Strasse 7, D-60438 Frankfurt am Main, Germany)
- Paola Fucini
(Frankfurt Institute for Molecular Life Sciences, Institute of Organic Chemistry and Chemical Biology, Goethe University Frankfurt, Max-von Laue-Strasse 7, D-60438 Frankfurt am Main, Germany)
- Thorsten Mielke
(Institut für Medizinische Physik und Biophysik, Charite – Universitätsmedizin Berlin, Ziegelstrasse 5–9, 10117-Berlin, Germany
UltraStrukturNetzwerk, Max Planck Institute for Molecular Genetics)
- Paul C. Whitford
(Theoretical Biology and Biophysics Group, Los Alamos National Laboratory)
- José N. Onuchic
(University of California)
- Yanan Yu
(Florida State University)
- Karissa Y. Sanbonmatsu
(Theoretical Biology and Biophysics Group, Los Alamos National Laboratory)
- Roland K. Hartmann
(Institut für Pharmazeutische Chemie, Philipps-Universität Marburg)
- Pawel A. Penczek
(The University of Texas – Houston Medical School, 6431 Fannin)
- Daniel N. Wilson
(Ludwig-Maximilians-Universität, Feodor-Lynenstrasse 25, 81377 München, Germany
Center for Integrated Protein Science, Ludwig-Maximilians-Universität München)
- Christian M. T. Spahn
(Institut für Medizinische Physik und Biophysik, Charite – Universitätsmedizin Berlin, Ziegelstrasse 5–9, 10117-Berlin, Germany)
Abstract
Turning heads on tRNA translocation on the ribosome During translation, transfer RNAs enter the ribosome and then move sequentially through three sites, known as A, P and E, as they transfer their attached amino acids onto the growing peptide chain. How the ribosome facilitates tRNA translocation between the sites remains largely unknown. Christian Spahn and colleagues have used multiparticle cryoelectron microscopy of a ribosome bound to the translation elongation factor, EF-G, to get information about tRNA movement. They identify two new sub-states and conclude that, following spontaneous inter-subunit ratcheting, translocation is the direct result of head swivelling and unratcheting of the 30S ribosomal subunit.
Suggested Citation
Andreas H. Ratje & Justus Loerke & Aleksandra Mikolajka & Matthias Brünner & Peter W. Hildebrand & Agata L. Starosta & Alexandra Dönhöfer & Sean R. Connell & Paola Fucini & Thorsten Mielke & Paul C. W, 2010.
"Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites,"
Nature, Nature, vol. 468(7324), pages 713-716, December.
Handle:
RePEc:nat:nature:v:468:y:2010:i:7324:d:10.1038_nature09547
DOI: 10.1038/nature09547
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