Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Peroxisomes01:24

Peroxisomes

Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
Peroxisomes01:24

Peroxisomes

Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
Peroxisomes01:30

Peroxisomes

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.The peroxisome is a single membrane-bound cellular organelle that can perform several different functions, including lipid metabolism and chemical detoxification. The enzymes within peroxisomes...
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
Exon Recombination02:32

Exon Recombination

The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon has three reading...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A chromosome-level genome assembly of Vanilla planifolia uncovers the genomic architecture underlying partial endoreplication.

BMC genomics·2026
Same author

P-GRe: An efficient pipeline for pseudogenes annotation.

Genomics·2026
Same author

Characterization of <i>Ralstonia pseudosolanacearum</i> phylotype I isolates causing bacterial wilt in Democratic Republic of Congo.

Plant disease·2026
Same author

The Marchantia polymorpha pangenome reveals ancient mechanisms of plant adaptation to the environment.

Nature genetics·2025
Same author

TBL38 atypical homogalacturonan-acetylesterase activity and cell wall microdomain localization in Arabidopsis seed mucilage secretory cells.

iScience·2024
Same author

Top five unanswered questions in plant cell surface research.

Cell surface (Amsterdam, Netherlands)·2024

Related Experiment Video

Updated: Jun 13, 2026

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
05:17

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

Published on: July 28, 2016

Evolution and expression of class III peroxidases.

Catherine Mathé1, Annick Barre, Cyril Jourda

  • 1Université de Toulouse, UPS, UMR 5546, Surfaces Cellulaires et Signalisation chez les Végétaux, BP 42617, F-31326 Castanet-Tolosan, France.

Archives of Biochemistry and Biophysics
|April 20, 2010
PubMed
Summary

Class III peroxidases, found only in plants, evolved with land plants but are present in earlier Streptophytes. Their conservation and copy number suggest roles in plant complexity and stress adaptation.

More Related Videos

Imaging of mtHyPer7, a Ratiometric Biosensor for Mitochondrial Peroxide, in Living Yeast Cells
09:47

Imaging of mtHyPer7, a Ratiometric Biosensor for Mitochondrial Peroxide, in Living Yeast Cells

Published on: June 2, 2023

Related Experiment Videos

Last Updated: Jun 13, 2026

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
05:17

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

Published on: July 28, 2016

Imaging of mtHyPer7, a Ratiometric Biosensor for Mitochondrial Peroxide, in Living Yeast Cells
09:47

Imaging of mtHyPer7, a Ratiometric Biosensor for Mitochondrial Peroxide, in Living Yeast Cells

Published on: June 2, 2023

Area of Science:

  • Plant Biology
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Class III peroxidases are a large, plant-specific multigenic family.
  • Their presence predates land colonization, appearing in basal Streptophytes.

Purpose of the Study:

  • To explore the evolutionary origins and potential functional significance of plant class III peroxidases.
  • To investigate the conservation and variability of class III peroxidase gene structures and sequences.

Main Methods:

  • Comparative analysis of class III peroxidase gene structures across plant lineages.
  • Examination of sequence conservation, including residues, motifs, and promoter regions.

Main Results:

  • Class III peroxidases are absent in Chlorophyta but present in Streptophytes, suggesting early land plant evolution links.
  • Gene structures show variability in intron number but conserved positions.
  • High copy number and conservation may relate to plant adaptation and complexity.
  • Conserved residues and motifs, alongside variable domains and low promoter identity, suggest isoform sub-functionalization.

Conclusions:

  • Plant class III peroxidases have deep evolutionary roots tied to land plant emergence.
  • Structural conservation and variability point to specialized functions within this large gene family.
  • Further research is needed to elucidate specific structure-function relationships among isoforms.