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10 results on '"Franckenberg, Sibylle"'

2. Localization of eukaryote-specific ribosomal proteins in a 5.5-Å cryo-EM map of the 80S eukaryotic ribosome

Author

Armache, Jean-Paul, Jarasch, Alexander, Anger, Andreas M., Villa, Elizabeth, Becker, Thomas, Bhushan, Shashi, Jossinet, Fabrice, Habeck, Michael, Dindar, Gülcin, Franckenberg, Sibylle, Marquez, Viter, Mielke, Thorsten, Thomm, Michael, Berninghausen, Otto, Beatrix, Birgitta, Söding, Johannes, Westhof, Eric, Wilson, Daniel N., Beckmann, Roland, and Blobel, Günter

Published
2010

3. Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution

Author

Armache, Jean-Paul, Jarasch, Alexander, Anger, Andreas M., Villa, Elizabeth, Becker, Thomas, Bhushan, Shashi, Jossinet, Fabrice, Habeck, Michael, Dindar, Gülcin, Franckenberg, Sibylle, Marquez, Viter, Mielke, Thorsten, Thomm, Michael, Berninghausen, Otto, Beatrix, Birgitta, Söding, Johannes, Westhof, Eric, Wilson, Daniel N., Beckmann, Roland, and Blobel, Gunter

Published
2010

4. Structural basis of highly conserved ribosome recycling in eukaryotes and archaea

Author

Becker, Thomas, Franckenberg, Sibylle, Wickles, Stephan, Shoemaker, Christopher J., Anger, Andreas M., Armache, Jean-Paul, Sieber, Heidemarie, Ungewickell, Charlotte, Berninghausen, Otto, Daberkow, Ingo, Karcher, Annette, Thomm, Michael, Hopfner, Karl-Peter, Green, Rachel, and Beckmann, Roland

Subjects
Ribosomes -- Structure -- Physiological aspects -- Research, Protein biosynthesis -- Physiological aspects -- Research, Eukaryotes -- Physiological aspects -- Research, Archaeabacteria -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Ribosome-driven protein biosynthesis is comprised of four phases: initiation, elongation, termination and recycling. In bacteria, ribosome recycling requires ribosome recycling factor and elongation factor G, and several structures of bacterial recycling complexes have been determined. In the eukaryotic and archaeal kingdoms, however, recycling involves the ABC-type ATPase ABCE1 and little is known about its structural basis. Here we present cryoelectron microscopy reconstructions of eukaryotic and archaeal ribosome recycling complexes containing ABCE1 and the termination factor paralogue Pelota. These structures reveal the overall binding mode of ABCE1 to be similar to canonical translation factors. Moreover, the iron-sulphur cluster domain of ABCE1 interacts with and stabilizes Pelota in a conformation that reaches towards the peptidyl transferase centre, thus explaining how ABCE1 may stimulate peptide-release activity of canonical termination factors. Using the mechanochemical properties of ABCE1, a conserved mechanism in archaea and eukaryotes is suggested that couples translation termination to recycling, and eventually to re-initiation., Recycling of ribosomes for a new round of translation initiation is an essential part of protein synthesis. In archaea and eukaryotes recycling has been shown to require the highly conserved [...]

Published
2012
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