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Related Concept Videos

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...
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,...
Diversity of Archaea IV01:29

Diversity of Archaea IV

Hyperthermophilic archaea are a group of extremophiles thriving at temperatures above 80°C, often in hydrothermal vents and volcanic soils where conditions surpass the boiling point of water. At such temperatures, proteins, membranes, and DNA in most organisms degrade, but hyperthermophiles have evolved remarkable adaptations to maintain stability and function.Unique Cellular FeaturesHyperthermophilic membranes are composed of a monolayer of biphytanyl tetraether lipids, which resist thermal...
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).
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
Mismatch Repair01:36

Mismatch Repair

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Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity
12:57

Alternative In Vitro Methods for the Determination of Viral Capsid Structural Integrity

Published on: November 16, 2017

First-step mutations for adaptation at elevated temperature increase capsid stability in a virus.

Kuo Hao Lee1, Craig R Miller, Anna C Nagel

  • 1Department of Physics, University of Idaho, Moscow, Idaho, United States of America.

Plos One
|October 8, 2011
PubMed
Summary

Most mutations in bacteriophage coat proteins adapting to heat are stabilizing, enhancing protein stability. This suggests elevated temperatures may drive adaptation by selecting for mutations that improve protein stability.

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Area of Science:

  • Molecular evolution
  • Protein biophysics
  • Virology

Background:

  • Mutations are crucial for molecular evolution and acquiring novel functions.
  • Mutations often decrease protein stability, posing challenges for adaptation.
  • Elevated temperatures might select for stabilizing mutations, preadapting proteins for new functions.

Purpose of the Study:

  • To investigate the impact of temperature adaptation on protein stability in bacteriophage mutations.
  • To determine if mutations arising during thermal adaptation are stabilizing or destabilizing.
  • To explore the role of protein-protein interactions in temperature adaptation.

Main Methods:

  • Analyzing single mutations in a G4-like bacteriophage adapting to elevated temperatures.
  • Utilizing molecular dynamic simulations to estimate thermodynamic stability changes.
  • Employing experimental decay assays to measure kinetic stability.

Main Results:

  • The majority of mutations occurred at interfaces between viral coat proteins, indicating effects on protein-protein interactions.
  • Most observed mutations were found to be stabilizing.
  • A small subset of mutations did not confer stability.

Conclusions:

  • Temperature adaptation in bacteriophages can be driven by stabilizing mutations.
  • Stabilizing mutations in coat proteins may enhance protein-protein interactions under thermal stress.
  • The study provides insights into the interplay between mutation, protein stability, and adaptation in viruses.