Related Experiment Video
Updated: May 17, 2026
05:37
Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
Published on: April 4, 2025
Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation.
Paola Cavaliere1, Bruno Pagano, Vincenzo Granata
1Dipartimento delle Scienze Biologiche, Università degli Studi di Napoli Federico II, Naples 80134, Italy.
Nucleic Acids Research
|October 30, 2012
Summary
Prion protein (PrP) interactions with quadruplex nucleic acids (NAs) were studied. PrP binds NAs with high affinity, suggesting a role in neurodegenerative diseases.
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- Prion protein (PrP) is implicated in neurodegenerative diseases.
- The interaction between PrP and nucleic acids (NAs) is not fully understood.
Purpose of the Study:
- To investigate the binding affinity and specificity of quadruplex-forming NAs with cellular and pathological PrP isoforms.
- To elucidate the structural basis and binding regions of PrP-NA interactions.
Main Methods:
- Isothermal titration calorimetry
- Surface plasmon resonance
- Circular dichroism
- Utilized various PrP forms and truncated mutants.
Main Results:
- Quadruplex NAs showed high affinity (62–630 nM K(D)) for PrP, with weaker binding to pathological PrP-β oligomers.
- The NA quadruplex architecture is crucial for PrP recognition.
- Both N-terminal and C-terminal domains of PrP are involved in NA binding.
- PrP-NA interaction induced reciprocal structural changes, suggesting PrP has quadruplex unwinding activity.
Conclusions:
- PrP exhibits high affinity and specific binding to quadruplex NAs.
- The quadruplex structure is key for PrP recognition, involving both PrP domains.
- PrP may possess in vivo quadruplex unwinding activity, potentially impacting its physiological and pathological roles.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...