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Related Concept Videos

Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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...
RNA Structure01:19

RNA Structure

The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...

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Related Experiment Video

Updated: Jun 26, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
11:19

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses

Published on: February 26, 2011

An active role for tRNA in decoding beyond codon:anticodon pairing.

Luisa Cochella1, Rachel Green

  • 1Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

Science (New York, N.Y.)
|May 21, 2005
PubMed
Summary
This summary is machine-generated.

A mutant transfer RNA (tRNA) accelerates its own acceptance into the ribosome, independent of codon pairing. This finding reveals tRNA

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De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data
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Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
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Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

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De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data
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De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data

Published on: February 18, 2022

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Transfer RNA (tRNA) selection is crucial for accurate protein synthesis.
  • Ribosome fidelity relies on discriminating cognate tRNAs from noncognate ones.
  • Discrimination involves differential dissociation rates and accelerated forward rate constants for cognate tRNAs.

Purpose of the Study:

  • To investigate the role of tRNA structure in its own acceptance during decoding.
  • To determine if tRNA can signal its acceptance independent of codon:anticodon interaction.

Main Methods:

  • Utilized a mutant tRNA(Trp) with a single D-arm substitution.
  • Assessed miscoding levels and forward rate constants.
  • Analyzed the impact of the mutation on tRNA acceptance independent of the decoding center.

Main Results:

  • The mutant tRNA(Trp) exhibited elevated miscoding levels.
  • The D-arm mutation accelerated forward rate constants for tRNA acceptance.
  • This acceleration was independent of codon:anticodon pairing in the decoding center.

Conclusions:

  • tRNA plays a direct role in signaling its own acceptance during ribosomal decoding.
  • The D-arm is a critical determinant for tRNA acceptance independent of codon recognition.
  • These findings support a fundamental role for tRNA in the evolution of protein synthesis.