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Related Concept Videos

SN2 Reaction: Stereochemistry02:23

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In an SN2 reaction, the nucleophilic attack on the substrate and departure of the leaving group occurs simultaneously through a transition state. As the nucleophile approaches the substrate from the back-side, the configuration of the substrate carbon changes from tetrahedral to trigonal bipyramidal and then back to tetrahedral, leading to an inversion in the configuration of the product.
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Repressed memories are a psychological phenomenon where memories of traumatic events are unconsciously blocked from a person's awareness. This process occurs as a defense mechanism, protecting the mind from the emotional impact of distressing or painful experiences. For example, a person who has experienced childhood trauma may grow up with no conscious recollection of the event. In such cases, the memories are thought to be buried deep within the subconscious, inaccessible to the conscious...
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RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
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This lesson provides an in-depth discussion of the stereochemical outcomes in an SN1 reaction.
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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Polycomb repressive complex 2 binds RNA irrespective of stereochemistry.

Charles E Deckard1, Jonathan T Sczepanski

  • 1Department of Chemistry, Texas A&M University, College Station, TX, USA. jon.sczepanski@chem.tamu.edu.

Chemical Communications (Cambridge, England)
|October 9, 2018
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Polycomb Repressive Complex 2 (PRC2) binds to both natural (d-RNA) and unnatural (l-RNA) G-quadruplex structures. This interaction, independent of stereochemistry, opens avenues for novel l-RNA-based PRC2 inhibitors.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • RNA Biology

Background:

  • Polycomb Repressive Complex 2 (PRC2) is a key epigenetic regulator involved in gene silencing.
  • PRC2 is known to interact with G-quadruplex (G4) RNA structures.
  • The stereochemistry of RNA interactions with native biological machinery is often considered critical.

Purpose of the Study:

  • To investigate the interaction of PRC2 with l-ribonucleic acids (l-RNA), the enantiomer of natural d-RNA.
  • To determine if PRC2's binding to G4 RNAs is stereochemistry-dependent.
  • To explore the potential of l-RNAs as therapeutic agents targeting PRC2.

Main Methods:

  • Synthesis and characterization of l-G4 RNAs.
  • Biochemical binding assays to assess PRC2-RNA interactions.
  • Competition assays to evaluate binding site occupancy.

Main Results:

  • PRC2 binds to l-G4 RNAs with similar affinity as d-G4 RNAs.
  • The interaction between PRC2 and G4 RNAs is independent of RNA stereochemistry.
  • l-G4 RNAs bind to the same site on PRC2 as d-RNAs and can outcompete them.

Conclusions:

  • PRC2 exhibits promiscuous binding to G4 RNAs, irrespective of their stereochemistry.
  • This finding challenges the notion that l-oligonucleotides are biologically inert.
  • Nuclease-resistant l-RNA molecules represent a promising new class of potential PRC2 inhibitors.