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  On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes - Delivered on 20 October 2002 at the 28th FEBS Meeting in Istanbul

Agmon, I., Auerbach, T., Baram, D., Bartels, H., Bashan, A., Berisio, R., et al. (2003). On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes - Delivered on 20 October 2002 at the 28th FEBS Meeting in Istanbul. European Journal of Biochemistry, 270(12), 2543-2556. doi:10.1046/j.1432-1033.2003.03634.x.

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Genre: Journal Article
Alternative Title : Eur. J. Biochem.

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 Creators:
Agmon, Ilana, Author
Auerbach, Tamar, Author
Baram, David, Author
Bartels, Heike, Author
Bashan, Anat, Author
Berisio, Rita1, Author           
Fucini, Paola1, Author           
Hansen, Harry A. S., Author
Harms, Jörg, Author
Kessler, Maggie, Author
Peretz, Moshe, Author
Schluenzen, Frank, Author
Yonath, Ada, Author
Zarivach, Raz, Author
Affiliations:
1Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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Free keywords: ribosomes; peptide bond formation; translocation; tunnel gating; elongation arrest
 Abstract: High-resolution crystal structures of large ribosomal subunits from Deinococcus radiodurans complexed with tRNA-mimics indicate that precise substrate positioning, mandatory for efficient protein biosynthesis with no further conformational rearrangements, is governed by remote interactions of the tRNA helical features. Based on the peptidyl transferase center (PTC) architecture, on the placement of tRNA mimics, and on the existence of a two-fold related region consisting of about 180 nucleotides of the 23S RNA, we proposed a unified mechanism integrating peptide bond formation, A-to-P site translocation, and the entrance of the nascent protein into its exit tunnel. This mechanism implies sovereign, albeit correlated, motions of the tRNA termini and includes a spiral rotation of the A-site tRNA-3' end around a local two-fold rotation axis, identified within the PTC. PTC features, ensuring the precise orientation required for the A-site nucleophilic attack on the P-site carbonyl-carbon, guide these motions. Solvent mediated hydrogen transfer appears to facilitate peptide bond formation in conjunction with the spiral rotation. The detection of similar two-fold symmetry-related regions in all known structures of the large ribosomal subunit, indicate the universality of this mechanism, and emphasizes the significance of the ribosomal template for the precise alignment of the substrates as well as for accurate and efficient translocation. The symmetry-related region may also be involved in regulatory tasks, such as signal transmission between the ribosomal features facilitating the entrance and the release of the tRNA molecules. The protein exit tunnel is an additional feature that has a role in cellular regulation. We showed by crystallographic methods that this tunnel is capable of undergoing conformational oscillations and correlated the tunnel mobility with sequence discrimination, gating and intracellular regulation.

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Language(s): eng - English
 Dates: 2003-06
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 174916
ISI: 000183348600001
DOI: 10.1046/j.1432-1033.2003.03634.x
 Degree: -

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Title: European Journal of Biochemistry
  Alternative Title : Eur. J. Biochem.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 270 (12) Sequence Number: - Start / End Page: 2543 - 2556 Identifier: ISSN: 0014-2956