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Ribozymes02:47

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
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Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the...
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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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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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Bacteriophages, also known as phages, are specialized viruses that infect bacteria. A key characteristic of phages is their distinctive “head-tail” morphology. A phage begins the infection process (i.e., lytic cycle) by attaching to the outside of a bacterial cell. Attachment is accomplished via proteins in the phage tail that bind to specific receptor proteins on the outer surface of the bacterium. The tail injects the phage’s DNA genome into the bacterial cytoplasm. In the...
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The Phlebovirus Ribonucleoprotein: An Overview.

François Ferron1,2, Julien Lescar3,4

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Methods in Molecular Biology (Clifton, N.J.)
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PubMed
Summary

Negative strand RNA viruses use ribonucleoproteins, not naked RNA, as templates for replication. Phlebovirus nucleocapsid structure and function are detailed, revealing insights into viral RNA binding and potential antiviral targets.

Keywords:
AssemblyLarge L proteinPhlebovirus nucleoproteinPolymeraseRNA replication

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Negative-strand RNA viruses rely on ribonucleoproteins (RNPs) for genome replication and transcription.
  • The nucleocapsid (N) protein is a key component of these RNPs, essential for encapsidating viral RNA (vRNA).

Purpose of the Study:

  • To provide an overview of the structure and function of phlebovirus ribonucleoproteins.
  • To elucidate the mechanisms of nucleocapsid monomer conformational changes and oligomerization.
  • To describe interactions between nucleocapsid proteins and viral RNA.

Main Methods:

  • Structural analysis of the nucleocapsid monomer.
  • Investigation of nucleocapsid-nucleocapsid oligomerization.
  • Analysis of nucleocapsid-viral RNA interactions.
  • Review of recent advances in tomography for studying N-L interactions.

Main Results:

  • The nucleocapsid monomer exhibits a flexible arm enabling conformational switching.
  • This switch facilitates transitions between a closed monomeric state and an open polymeric state.
  • The open state is competent for viral RNA binding and encapsidation.
  • Specific modes of N-N oligomerization and vRNA interactions are described.

Conclusions:

  • The structural flexibility of the nucleocapsid protein is crucial for its function in viral RNA encapsidation.
  • Understanding these interactions provides a basis for designing specific antiviral compounds targeting phleboviruses.
  • Advances in tomography offer new avenues for studying N-L interactions and developing antivirals.