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Improving Translational Accuracy

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.Ribosome Structure and AssemblyRibosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within the...

Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within...

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
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Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.Ribosome Structure and AssemblyRibosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within the...

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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...

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Related Experiment Video

Updated: Jun 13, 2026

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

eEF1A: thinking outside the ribosome.

Maria K Mateyak¹, Terri Goss Kinzy

¹Department of Molecular Genetics, Microbiology and Immunology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854-5635, USA.

The Journal of Biological Chemistry

|May 7, 2010

Summary

Eukaryotic translation elongation factor 1A (eEF1A) is crucial for protein synthesis and has diverse non-canonical functions. Understanding these roles offers insights into viral interactions and cellular organization.

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Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Eukaryotic translation elongation factor 1A (eEF1A) is a highly abundant protein synthesis factor.
It facilitates the delivery of aminoacyl-tRNAs to the ribosome during protein elongation.
eEF1A exhibits numerous unique cellular and viral activities beyond its canonical role in translation.

Purpose of the Study:

To explore the multifaceted roles of eEF1A.
To understand the non-canonical functions of eEF1A in various biological processes.
To elucidate the mechanistic basis of eEF1A's diverse activities.

Main Methods:

Literature review of biochemical and biological interactions of eEF1A.
Analysis of studies investigating eEF1A's involvement in cellular and viral processes.
Synthesis of current knowledge on eEF1A's non-canonical functions.

Main Results:

eEF1A has been linked to a wide array of functions beyond protein synthesis.
These functions span from viral-host interactions to subcellular organization.
eEF1A is implicated in integrating key cellular pathways.

Conclusions:

eEF1A possesses a remarkable diversity of functions, exceeding those of other translation factors.
Mechanistic understanding of eEF1A's non-canonical roles is vital for addressing key biological questions.
Further research into eEF1A will illuminate viral-host dynamics, cellular organization, and pathway integration.