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Related Concept Videos

Nuclear Export of mRNA02:31

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In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing...
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The structure and stability of mRNA molecules regulates gene expression, as mRNAs are a key step in the pathway from gene to protein. In eukaryotes, the half-life of mRNA varies from a few minutes up to several days. mRNA stability is essential in growth and development. The absence of the proteins regulating its stability, such as tristetraprolin in mice, can cause systemic issues, including bone marrow overgrowth, inflammation, and autoimmunity.
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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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Small interfering RNAs, or siRNAs, are short regulatory RNA molecules that can silence genes post-transcriptionally, as well as the transcriptional level in some cases. siRNAs are important for protecting cells against viral infections and silencing transposable genetic elements.
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Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection
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Inhibition of mRNA nuclear export promotes SARS-CoV-2 pathogenesis.

Menghan Mei1, Anastasija Cupic2,3, Lisa Miorin2,4

  • 1Department of Biochemistry, Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.

Proceedings of the National Academy of Sciences of the United States of America
|May 20, 2024
PubMed
Summary

Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) nonstructural protein 1 (Nsp1) uses an acidic N-terminal patch to bind NXF1, inhibiting host mRNA export and promoting viral virulence.

Keywords:
NXF1Nsp1SARS-CoV-2mRNA exportnuclear transport

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Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • SARS-CoV-2 nonstructural protein 1 (Nsp1) is a key virulence factor.
  • Nsp1 inhibits host gene expression and antiviral responses.
  • Mechanisms of Nsp1 virulence functions are not fully understood.

Purpose of the Study:

  • To elucidate the mechanism of Nsp1-mediated inhibition of mRNA export.
  • To identify the specific Nsp1 interaction site with the NXF1-NXT1 mRNA export receptor.
  • To determine the role of Nsp1-NXF1 interaction in SARS-CoV-2 replication and pathogenicity.

Main Methods:

  • Nsp1 mutagenesis based on crystal structure.
  • Photoactivatable Nsp1 probe assay.
  • Generation of recombinant SARS-CoV-2 mutant virus.
  • In vivo pathogenicity studies.

Main Results:

  • An acidic N-terminal patch on Nsp1 is critical for NXF1-NXT1 interaction.
  • The RNA Recognition Motif (RRM) domain of NXF1 is an Nsp1 binding site.
  • A separation-of-function Nsp1 mutant lost NXF1 interaction but retained translation inhibition.
  • Nsp1 N-terminal acidic patch is essential for inhibiting host mRNA export, viral replication, and pathogenicity in vivo.

Conclusions:

  • Nsp1 directly targets the NXF1-NXT1 mRNA export pathway.
  • The Nsp1 N-terminal acidic patch is a crucial determinant of SARS-CoV-2 virulence.
  • Inhibition of host mRNA export by Nsp1 is vital for viral replication and pathogenicity.