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  The E-site story: the importance of maintaining two tRNAs on the ribosome during protein synthesis

Wilson, D. N., & Nierhaus, K. (2006). The E-site story: the importance of maintaining two tRNAs on the ribosome during protein synthesis. Cellular and Molecular Life Sciences, 63(23), 2725-2737. doi:10.1007/s00018-006-6125-4.

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Genre: Journal Article
Alternative Title : CMLS

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 Creators:
Wilson, Daniel N.1, Author           
Nierhaus, Knud2, Author           
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1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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Free keywords: Protein synthesis - tRNA binding sites - A site - E site - accuracy of protein synthesis - frameshift
 Abstract: In the sixties James Watson suggested a twosite model for the ribosome comprising the P site for the peptidyl transfer RNA (tRNA) before peptide-bond formation and the A site, where decoding takes place according to the codon exposed there. In the eighties a third tRNA binding site was detected, the E site, which was specific for deacylated tRNA and turned out to be a universal feature of ribosomes. However, despite having three tRNA binding sites, only two tRNAs occupy the ribosome at a time during protein synthesis: at the A and P sites before translocation (PRE state) and at the P and E sites after translocation (POST state). The importance of having two tRNAs in the POST state has been revealed during the last 25 years, showing that the E site contributes two fundamental features: (i) the fact that incorporation of a wrong amino acid is not harmful for the cell (only 1 in about 400 misincorporations destroys the function of a protein) stems from the presence of an E-tRNA; (ii) maintenance of the reading frame is one of the most remarkable achievements of the ribosome, essential for faithful translation of the genetic information. The presence of the POST state E-tRNA prevents

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Language(s): eng - English
 Dates: 2006-12-01
 Publication Status: Issued
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 Identifiers: eDoc: 305641
DOI: 10.1007/s00018-006-6125-4
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Title: Cellular and Molecular Life Sciences
  Alternative Title : CMLS
Source Genre: Journal
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Pages: - Volume / Issue: 63 (23) Sequence Number: - Start / End Page: 2725 - 2737 Identifier: ISSN: 1420-682X