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Related Concept Videos

Improving Translational Accuracy02:07

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...
Initiation of Translation02:33

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...

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Related Experiment Video

Updated: May 21, 2026

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics
09:52

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics

Published on: September 15, 2020

In vitro trans-translation assays.

Daisuke Kurita1, Akira Muto, Hyouta Himeno

  • 1Department of Biochemistry and Molecular Biology, Hirosaki University, Hirosaki, Japan.

Methods in Molecular Biology (Clifton, N.J.)
|June 28, 2012
PubMed
Summary

Trans-translation, a bacterial protein quality control system, uses transfer-messenger RNA (tmRNA). This study details an in vitro system to analyze tmRNA

Area of Science:

  • Molecular Biology
  • Bacterial Protein Synthesis
  • Cellular Quality Control

Background:

  • Protein synthesis quality control is crucial for bacterial survival.
  • Trans-translation, mediated by tmRNA, rescues stalled ribosomes.
  • Understanding trans-translation mechanism is key to bacterial biology.

Purpose of the Study:

  • To establish an in vitro system for studying bacterial trans-translation.
  • To dissect the two key steps of the trans-translation process.
  • To analyze peptidyl-transfer and resume codon decoding.

Main Methods:

  • Purified protein factors were utilized.
  • An in vitro reconstituted system was employed.
  • Biochemical assays were performed to evaluate trans-translation steps.

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Quantitative Immunofluorescence to Measure Global Localized Translation
09:13

Quantitative Immunofluorescence to Measure Global Localized Translation

Published on: August 22, 2017

Related Experiment Videos

Last Updated: May 21, 2026

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics
09:52

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics

Published on: September 15, 2020

In Vitro Transcribed RNA-based Luciferase Reporter Assay to Study Translation Regulation in Poxvirus-infected Cells
08:58

In Vitro Transcribed RNA-based Luciferase Reporter Assay to Study Translation Regulation in Poxvirus-infected Cells

Published on: May 1, 2019

Quantitative Immunofluorescence to Measure Global Localized Translation
09:13

Quantitative Immunofluorescence to Measure Global Localized Translation

Published on: August 22, 2017

Main Results:

  • The study successfully reconstituted the trans-translation system in vitro.
  • Peptidyl-transfer from peptidyl-tRNA to alanyl-tmRNA was characterized.
  • Decoding of the tmRNA resume codon was evaluated.

Conclusions:

  • The described in vitro system allows for detailed mechanistic studies of trans-translation.
  • This system provides a platform for future investigations into bacterial protein quality control.
  • Further research can elucidate the regulation and function of trans-translation.