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Related Concept Videos

Leaky Scanning02:28

Leaky Scanning

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 stands for...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
Initiation of Translation02:33

Initiation of Translation

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...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

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...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

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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Related Experiment Video

Updated: Jul 2, 2026

Imaging ATG9A, a Multi-Spanning Membrane Protein
07:20

Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

ATG9A is an essential host factor for parechovirus RNA replication.

You Li1, Lorellin A Durnell-Bettis1, Fahmida Alam2

  • 1Department of Pediatrics, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.

Journal of Virology
|July 1, 2026
PubMed
Summary

Parechovirus A3 (PeV-A3) infection in newborns is poorly understood. A CRISPR screen identified ATG9A as essential for PeV replication, independent of autophagy, revealing a new target for antiviral therapies.

Keywords:
ATG2ATG9AGolgiautophagyparechoviruspicornavirus

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Last Updated: Jul 2, 2026

Imaging ATG9A, a Multi-Spanning Membrane Protein
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Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus
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Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus

Published on: October 7, 2011

Preparation of rAAV9 to Overexpress or Knockdown Genes in Mouse Hearts
11:11

Preparation of rAAV9 to Overexpress or Knockdown Genes in Mouse Hearts

Published on: December 17, 2016

Area of Science:

  • Virology
  • Molecular Biology
  • Genetics

Background:

  • Parechoviruses (PeVs), particularly PeV-A3, cause severe neonatal sepsis and meningoencephalitis.
  • The viral life cycle and pathogenesis of PeV-A3 are not well understood.
  • Identifying host factors is crucial for understanding PeV-A3 infection and developing treatments.

Purpose of the Study:

  • To identify host factors essential for PeV-A3 replication using a genome-wide CRISPR screen.
  • To elucidate the role of identified host factors in the PeV-A3 life cycle.
  • To explore potential therapeutic targets for PeV-A3 infection.

Main Methods:

  • Genome-wide CRISPR screening to identify host factors for PeV-A3 replication.
  • Assays to determine the necessity of host factors for viral entry, translation, and RNA replication.
  • Co-localization studies using double-stranded RNA (dsRNA) as a marker for viral replication organelles (ROs).

Main Results:

  • A set of Golgi-localized proteins, including the lipid scramblase ATG9A, were found to be essential for PeV infection across genotypes.
  • ATG9A is critical for PeV-A3 viral RNA replication, independent of canonical autophagy.
  • ATG9A co-localizes with dsRNA within ROs, and the ATG2-ATG9A complex is required for optimal viral replication.

Conclusions:

  • The ATG2-ATG9A complex plays a vital role in PeV-A3 replication by potentially delivering lipids to ROs.
  • ATG9A's function in viral RNA replication offers a novel target for antiviral drug development against PeV-A3.
  • This study provides critical insights into the molecular mechanisms underlying PeV pathogenesis.