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Related Concept Videos

Mutations in Microorganisms01:18

Mutations in Microorganisms

Mutations are heritable changes in an organism’s genome involving alterations in the base sequence of DNA or RNA. These changes can influence cellular processes and phenotypic traits, potentially transforming the unaltered wild type into a mutant form. Such changes, termed forward mutations, are pivotal in shaping the genetic diversity of organisms.RNA viruses exhibit the highest mutation rates due to the absence of robust proofreading mechanisms during genome replication. In contrast,...
Viral Mutations00:36

Viral Mutations

A mutation is a change in the sequence of bases of DNA or RNA in a genome. Some mutations occur during replication of the genome due to errors made by the polymerase enzymes that replicate DNA or RNA. Unlike DNA polymerase, RNA polymerase is prone to errors because it is not capable of “proofreading” its work. Viruses with RNA-based genomes, like HIV, therefore accrue mutations faster than viruses with DNA-based genomes. Because mutation and recombination provide the raw material for adaptive...
Spontaneous and Induced Mutations01:30

Spontaneous and Induced Mutations

Spontaneous mutations arise infrequently during DNA replication due to errors in the process. A key factor behind these errors is tautomeric shifts in nitrogenous bases, where bases transition from keto to enol forms or amino to imino forms. This shift can alter base-pairing rules, leading to mutations. Additionally, reactive oxygen species (ROS) arising from aerobic metabolism can damage DNA, resulting in depurination (loss of a purine base) or depyrimidination (loss of a pyrimidine base).
Mutations01:35

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...
Mutations01:39

Mutations

Overview
Mutations01:39

Mutations

Overview

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Related Experiment Video

Updated: May 10, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Changes in prion replication environment cause prion strain mutation.

Nuria Gonzalez-Montalban1, Young Jin Lee, Natallia Makarava

  • 1Center for Biomedical Engineering and Technology, University of Maryland School of Medicine, 725 W. Lombard St., Baltimore, MD 21201, USA.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|June 5, 2013
PubMed
Summary
This summary is machine-generated.

Changes in the prion replication environment, not just primary structure, can cause prion strain mutations. This study shows RNA content alterations induce novel prion conformations with altered stability and replication rates.

Keywords:
amyloidconformational stabilityneurodegenerative diseasesprotein misfoldingprotein misfolding cyclic amplificationproteinase K digestion

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Area of Science:

  • Prion biology
  • Molecular biology
  • Biochemistry

Background:

  • Interspecies prion transmission can cause prion strain mutations, altering their physical and biological traits.
  • The role of the replication environment, independent of PrP primary structure changes, in prion strain mutation remains unclear.

Purpose of the Study:

  • To investigate whether alterations in the prion replication environment can induce prion strain mutations without changing the PrP primary structure.
  • To explore the impact of RNA content on prion conformation and replication.

Main Methods:

  • Serial protein misfolding cyclic amplification (sPMCAb) was used to amplify hamster prion strains.
  • RNA content was manipulated during the amplification process, including adaptation to RNA-depleted and RNA-containing environments.

Main Results:

  • A novel PrP(Sc) conformation, 263K(R+), emerged in strain 263K after adaptation to an RNA-depleted and subsequent RNA-containing environment.
  • The 263K(R+) conformation exhibited significantly lower stability, higher proteolytic sensitivity, and a vastly increased replication rate compared to the original 263K strain.
  • Similar transformations were observed in strain Hyper, indicating the phenomenon is not unique to 263K.
  • The novel conformation emerged de novo due to RNA content changes, not present in the original brain-derived material.

Conclusions:

  • Dramatic transformations in PrP(Sc) conformation can be induced by altering the prion replication environment, specifically RNA content.
  • Prion strain mutations can occur without any changes in the prion protein's primary amino acid sequence.
  • This finding broadens the understanding of prion strain diversity and evolution mechanisms.