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  Structure and dynamics of the mammalian ribosomal pretranslocation complex

Budkevich, T., Giesebrecht, J., Altman, R. B., Munro, J. B., Mielke, T., Nierhaus, K. H., et al. (2011). Structure and dynamics of the mammalian ribosomal pretranslocation complex. Mol Cell, 44(2), 214-24. Retrieved from http://pdn.sciencedirect.com/science?_ob=MiamiImageURL&_cid=272198&_user=28761&_pii=S109727651100757X&_check=y&_origin=article&_zone=toolbar&_coverDate=21-Oct-2011&view=c&originContentFamily=serial&wchp=dGLzVlt-zSkzS&md5=7955fd02fcf620b68260bfdefd7032ae/1-s2.0-S109727651100757X-main.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-77F8-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-77F9-8
Genre: Journal Article

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 Creators:
Budkevich, T.1, Author              
Giesebrecht, J., Author
Altman, R. B., Author
Munro, J. B., Author
Mielke, T.2, Author              
Nierhaus, K. H.3, Author              
Blanchard, S. C., Author
Spahn, C. M.4, Author              
Affiliations:
1Dept. of Human Molecular Genetics (Head: Hans-Hilger Ropers), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433549              
2Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
3Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              
4Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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Free keywords: Animals; Anti-Bacterial Agents/chemistry; Binding Sites; Cryoelectron Microscopy; Cycloheximide/chemistry; Fluorescence Resonance Energy Transfer; Models, Molecular; Nucleic Acid Conformation; RNA, Transfer, Amino Acyl/ chemistry/metabolism; Rabbits; Ribosomes/ chemistry/metabolism
 Abstract: Although the structural core of the ribosome is conserved in all kingdoms of life, eukaryotic ribosomes are significantly larger and more complex than their bacterial counterparts. The extent to which these differences influence the molecular mechanism of translation remains elusive. Multiparticle cryo-electron microscopy and single-molecule FRET investigations of the mammalian pretranslocation complex reveal spontaneous, large-scale conformational changes, including an intersubunit rotation of the ribosomal subunits. Through structurally related processes, tRNA substrates oscillate between classical and at least two distinct hybrid configurations facilitated by localized changes in their L-shaped fold. Hybrid states are favored within the mammalian complex. However, classical tRNA positions can be restored by tRNA binding to the E site or by the eukaryotic-specific antibiotic and translocation inhibitor cycloheximide. These findings reveal critical distinctions in the structural and energetic features of bacterial and mammalian ribosomes, providing a mechanistic basis for divergent translation regulation strategies and species-specific antibiotic action.

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 Dates: 2011
 Publication Status: Published in print
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Title: Mol Cell
Source Genre: Journal
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Pages: - Volume / Issue: 44 (2) Sequence Number: - Start / End Page: 214 - 24 Identifier: ISSN: 1097-4164 (Electronic) 1097-2765 (Linking)