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Transfer RNA Synthesis02:36

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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.
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
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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.
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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.
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tREPs-A New Class of Functional tRNA-Encoded Peptides.

Amrita Chakrabarti1,2, Monika Kaushik3, Juveria Khan3

  • 1Department of Life Sciences, Shiv Nadar University, Greater Noida 201314, Uttar Pradesh, India.

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|June 13, 2022
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Summary

Researchers synthesized novel tRNA-encoded peptides (tREPs) from Escherichia coli, discovering tREP-18 exhibits potent antileishmanial activity by disrupting parasite structure and function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Parasitology

Background:

  • Transfer RNA (tRNA) sequences are primarily known for their role in protein synthesis.
  • The potential for tRNA sequences to encode functional peptides (tREPs) has been largely unexplored.

Purpose of the Study:

  • To investigate the potential for tRNA sequences to encode functional peptides.
  • To artificially synthesize and characterize novel tREPs for therapeutic applications.
  • To identify and validate tREPs with antiparasitic activity.

Main Methods:

  • Computational translation of Escherichia coli tRNA sequences into hypothetical tREP sequences.
  • Bioinformatic filtering (sequence, structure, energy) to select candidate tREPs.
  • Chemical synthesis of selected tREPs, including tREP-18.
  • In vitro antileishmanial assays against Leishmania donovani strains (Ag83 and BS12).
  • Microscopy (AFM, SEM) to assess structural changes in parasites.
  • Mitochondrial membrane potential assays.

Main Results:

  • A database of hypothetical tREPs was generated from E. coli tRNA sequences.
  • The synthesized tREP-18 demonstrated potent antileishmanial activity against Leishmania donovani (IC50 = 22.13 nM for Ag83, 15 nM for BS12).
  • tREP-18 induced significant alterations in parasite cytoskeletal architecture and destabilized mitochondrial membrane potential.
  • tREP-18 showed efficacy against the amastigote stage and promoted macrophage pathogen clearance.

Conclusions:

  • This study provides proof-of-concept for generating a new class of functional peptides from tRNA sequences.
  • tREP-18 represents a novel, potent antileishmanial agent with a unique mechanism of action.
  • The exploration of tRNA-peptide space offers a vast, untapped resource for discovering novel therapeutic agents.