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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...
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The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Related Experiment Video

Updated: Jun 3, 2025

In Vitro Transcribed RNA-based Luciferase Reporter Assay to Study Translation Regulation in Poxvirus-infected Cells
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Ribosome customization and functional diversification among P-stalk proteins regulate late poxvirus protein

Natalia Khalatyan1, Daphne Cornish2, Aaron J Ferrell3

  • 1Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.

Cell Reports
|January 9, 2025
PubMed
Summary

Poxviruses alter ribosome structure to control protein synthesis. Specific ribosomal proteins (RPs) become essential for translating viral late mRNAs, highlighting a novel virus-host interaction.

Keywords:
CP: Molecular biologyCRISPR screenP-stalkRACK1RPLP2cryo-EMpoxvirusribosome customizationtranslational control

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Area of Science:

  • Molecular Biology
  • Virology
  • Structural Biology

Background:

  • Ribosomes selectively regulate translation of specific messenger RNA (mRNA) subsets.
  • Poxviruses are large DNA viruses with complex replication strategies.

Purpose of the Study:

  • To investigate how poxvirus infection affects ribosome composition and function.
  • To identify specific ribosomal proteins (RPs) involved in poxvirus mRNA translation.

Main Methods:

  • Quantitative proteomics to analyze ribosomal protein composition.
  • Cryo-electron microscopy to determine structural changes in ribosomes.
  • Genetic knockout screens and metabolic assays to assess RP function.
  • Dual-reporter virus assays to study viral mRNA translation.

Main Results:

  • Poxvirus infection did not alter overall ribosomal subunit protein (RP) composition.
  • Infection induced structural changes in 40S ribosomal subunits, including altered rotation states and displaced head domains.
  • Receptor of activated C kinase 1 (RACK1) and RPLP2 were identified as RPs crucial for non-canonical translation of late poxvirus mRNAs.
  • RPLP2, a subunit of the P-stalk, was specifically required for poxvirus protein synthesis, while RPLP1 was dispensable.

Conclusions:

  • Poxviruses structurally customize host ribosomes to favor their own mRNA translation.
  • The virus becomes reliant on traditionally non-essential RPs, such as RACK1 and RPLP2, for efficient initiation on late viral mRNAs.
  • This study reveals a sophisticated mechanism of viral translation control involving ribosome structural adaptation.