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Related Concept Videos

Ribosomes01:27

Ribosomes

67.7K
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...
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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
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Initiation of Translation02:33

Initiation of Translation

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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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Leaky Scanning02:28

Leaky Scanning

5.1K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.1K
Improving Translational Accuracy02:07

Improving Translational Accuracy

10.1K
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...
10.1K
tRNA Activation02:26

tRNA Activation

19.2K
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 24, 2025

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

Published on: August 1, 2016

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Engineering Ribosomal Machinery for Noncanonical Amino Acid Incorporation.

Satoshi Ishida1, Phuoc H T Ngo1, Arno Gundlach1

  • 1Department of Molecular Biosciences, University of Texas at Austin, Austin, Texas 78712, United States.

Chemical Reviews
|June 3, 2024
PubMed
Summary
This summary is machine-generated.

Researchers are engineering the ribosome and its associated factors to incorporate noncanonical amino acids into proteins, enabling new genetic code modifications. This work advances protein engineering and synthetic biology.

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Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
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Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
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Related Experiment Videos

Last Updated: Jun 24, 2025

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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Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
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Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
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Area of Science:

  • Synthetic Biology
  • Molecular Biology
  • Protein Engineering

Background:

  • Noncanonical amino acids (ncAAs) allow modification of protein properties.
  • Genetic code alteration relies on orthogonal aminoacyl-tRNA synthetase:tRNA pairs.
  • Translation machinery components are key to developing novel genetic codes.

Purpose of the Study:

  • To review recent advances in engineering ribosomal machinery for ncAAs.
  • To discuss modifications to the ribosome, tRNAs, and accessory factors like EF-Tu.
  • To explore future directions for genetic code alteration through translation machinery engineering.

Main Methods:

  • Review of literature on ribosome engineering.
  • Analysis of tRNA and accessory factor interactions with the ribosome.
  • Discussion of genome re-engineering successes and future requirements.

Main Results:

  • Significant progress has been made in engineering ribosomal machinery for ncAAs.
  • The ribosome, tRNAs, and factors like EF-Tu are crucial targets for modification.
  • Expansive alterations in translation machinery are necessary for radical genetic code changes.

Conclusions:

  • Engineering the translation machinery is vital for expanding the genetic code.
  • Future protein engineering relies on advanced ribosome and tRNA modifications.
  • Synthetic biology approaches offer new avenues for protein functionalization.