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Related Concept Videos

tRNA Activation02:26

tRNA Activation

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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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tRNA Activation02:26

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Transfer RNA Synthesis02:36

Transfer RNA Synthesis

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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...
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Transfer RNA Synthesis02:35

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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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Related Experiment Video

Updated: Mar 28, 2026

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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tRNAs taking charge.

Jonathan W Cruz1, Nancy A Woychik2

  • 1Department of Biochemistry and Molecular Biology, Rutgers University, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.

Pathogens and Disease
|December 15, 2015
PubMed
Summary

Bacterial toxin-antitoxin (TA) systems protect cells from stress by halting growth. New research reveals these toxins cleave tRNAs, not just mRNAs, offering a novel perspective on their function and stress response parallels.

Keywords:
Rny1VapCangiogeninantitoxintoxintranslation inhibition

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Genetics

Background:

  • Bacterial toxin-antitoxin (TA) systems are chromosomally encoded.
  • TA toxins induce reversible growth arrest to protect cells from stress.
  • Traditionally, TA toxins were thought to inhibit protein synthesis by cleaving mRNA.

Purpose of the Study:

  • To investigate the RNA targets of toxin-antitoxin toxins in Mycobacterium tuberculosis.
  • To explore novel mechanisms of toxin-mediated translation inhibition.
  • To understand the role of TA systems in bacterial stress response.

Main Methods:

  • Development and application of a specialized RNA sequencing (RNA-seq) method.
  • Study of toxin-antitoxin systems in Mycobacterium tuberculosis.
  • Analysis of toxin-induced RNA cleavage products.

Main Results:

  • Identification of tRNA cleavage by TA toxins, producing tRNA halves.
  • Demonstration that TA toxins target specific tRNAs in addition to mRNA.
  • Uncovering a novel mechanism of translation inhibition by TA toxins.

Conclusions:

  • Mycobacterium tuberculosis TA toxins cleave tRNAs, generating tRNA halves.
  • This finding expands the known targets of TA toxins beyond mRNA.
  • The mechanism reveals parallels with eukaryotic stress response pathways.