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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. 
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Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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Biochemical Principles in Prion-Based Inheritance.

Emily M Dennis1, David M Garcia2

  • 1Department of Chemistry and Biochemistry, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.

Epigenomes
|February 28, 2022
PubMed
Summary
This summary is machine-generated.

Prions are proteins with unique self-templating abilities, leading to heritable changes. Recent discoveries reveal their widespread presence and beneficial roles, expanding our understanding of epigenetics.

Keywords:
amyloidepigeneticsprionprion-likeprotein aggregationtransgenerational inheritance

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Prions are proteins capable of adopting alternative structures with altered activities.
  • These altered structures can self-template, leading to inheritance across cell divisions and generations.
  • Despite decades of study, prion discovery has been limited due to their complex nature.

Purpose of the Study:

  • To review the biochemical principles of prion proteins, including sequences, characteristics, and structures.
  • To summarize current knowledge on prion self-templating mechanisms.
  • To provide a framework for defining prions as new examples emerge.

Main Methods:

  • Literature review of prion protein biochemistry.
  • Analysis of prion sequences, characteristics, and structures.
  • Examination of prion self-templating mechanisms across organisms.

Main Results:

  • Prions are widespread in nature and can confer beneficial phenotypes.
  • Significant advancements in understanding prion structures and inheritance modes have been made.
  • Prion-based inheritance represents an understudied area of epigenetics.

Conclusions:

  • Prions are fundamental molecules with diverse roles and inheritance mechanisms.
  • A biochemical foundation is essential for defining and identifying new prions.
  • Further research into prion-based inheritance will deepen our understanding of epigenetics.