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  SecM-stalled ribosomes adopt an altered geometry at the peptidyl transferase center

Bhushan, S., Hoffmann, T., Seidelt, B., Frauenfeld, J., Mielke, T., Berninghausen, O., et al. (2011). SecM-stalled ribosomes adopt an altered geometry at the peptidyl transferase center. PLoS Biology, 9(1), e1000581. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/21267063 http://www.plosbiology.org/article/fetchObjectAttachment.action?uri=info%3Adoi%2F10.1371%2Fjournal.pbio.1000581&representation=PDF.

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Bhushan, S., Author
Hoffmann, T., Author
Seidelt, B., Author
Frauenfeld, J., Author
Mielke, T.1, Author              
Berninghausen, O., Author
Wilson, D. N.2, Author              
Beckmann, R., Author
Affiliations:
1Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
2Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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Free keywords: Catalytic Domain; Cryoelectron Microscopy; Escherichia coli/*enzymology; Escherichia coli Proteins/*chemistry/metabolism; Molecular Conformation; Peptidyl Transferases/*chemistry/metabolism; Protein Biosynthesis; Protein Structure, Quaternary; Protein Structure, Tertiary; RNA, Transfer/chemistry/metabolism; Ribosomes/*chemistry/metabolism; Transcription Factors/*chemistry/metabolism
 Abstract: As nascent polypeptide chains are synthesized, they pass through a tunnel in the large ribosomal subunit. Interaction between specific nascent chains and the ribosomal tunnel is used to induce translational stalling for the regulation of gene expression. One well-characterized example is the Escherichia coli SecM (secretion monitor) gene product, which induces stalling to up-regulate translation initiation of the downstream secA gene, which is needed for protein export. Although many of the key components of SecM and the ribosomal tunnel have been identified, understanding of the mechanism by which the peptidyl transferase center of the ribosome is inactivated has been lacking. Here we present a cryo-electron microscopy reconstruction of a SecM-stalled ribosome nascent chain complex at 5.6 A. While no cascade of rRNA conformational changes is evident, this structure reveals the direct interaction between critical residues of SecM and the ribosomal tunnel. Moreover, a shift in the position of the tRNA-nascent peptide linkage of the SecM-tRNA provides a rationale for peptidyl transferase center silencing, conditional on the simultaneous presence of a Pro-tRNA(Pro) in the ribosomal A-site. These results suggest a distinct allosteric mechanism of regulating translational elongation by the SecM stalling peptide.

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 Dates: 2011
 Publication Status: Published in print
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Title: PLoS Biology
Source Genre: Journal
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Pages: - Volume / Issue: 9 (1) Sequence Number: - Start / End Page: e1000581 Identifier: ISSN: 1545-7885 (Electronic) 1544-9173 (Linking)