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

Proteomics01:33

Proteomics

9.2K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
9.2K
The Proteasome Structure01:17

The Proteasome Structure

1.6K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
1.6K
The Proteasome02:18

The Proteasome

10.0K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
10.0K
The Proteasome01:13

The Proteasome

1.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.6K

You might also read

Related Articles

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

Sort by
Same author

Evolutionary and Biochemical Perspectives on the Incorporation and Utilization of Selenocysteine.

Cold Spring Harbor perspectives in biology·2026
Same author

Regulatory landscape of widespread stop codon readthrough in <i>Drosophila</i>.

bioRxiv : the preprint server for biology·2026
Same author

Tracing the vertebrate selenoproteome evolution reveals expansions in ray-finned fishes and convergent depletions in tetrapods.

BMC genomics·2026
Same author

Three-Year Cereal: Field Bean Intercropping Greatly Reduced Weed Abundance with Small Changes in Functional Composition.

Biology·2026
Same author

Overcoming the widespread flaws in the annotation of vertebrate selenoprotein genes in public databases.

PLoS computational biology·2026
Same author

Translon: a single term for translated regions.

Nature methods·2025

Related Experiment Video

Updated: Jan 11, 2026

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
03:09

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

1.3K

The Metazoan Selenoproteome.

Max Ticó1,2, Marco Mariotti1

  • 1Department of Genetics, Microbiology and Statistics, Universitat de Barcelona, Barcelona, Catalonia, Spain;

Annual Review of Animal Biosciences
|November 10, 2025
PubMed
Summary

Selenoproteins use the amino acid selenocysteine (Sec) for vital functions. Their evolution across animals shows diverse gene gains and losses, impacting crucial biological pathways.

Keywords:
evolutionrecodingredoxseleniumselenocysteineselenoprotein

More Related Videos

An Aquatic Microbial Metaproteomics Workflow: From Cells to Tryptic Peptides Suitable for Tandem Mass Spectrometry-based Analysis
08:09

An Aquatic Microbial Metaproteomics Workflow: From Cells to Tryptic Peptides Suitable for Tandem Mass Spectrometry-based Analysis

Published on: September 15, 2015

9.2K
Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS
17:12

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS

Published on: December 20, 2010

16.0K

Related Experiment Videos

Last Updated: Jan 11, 2026

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
03:09

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

1.3K
An Aquatic Microbial Metaproteomics Workflow: From Cells to Tryptic Peptides Suitable for Tandem Mass Spectrometry-based Analysis
08:09

An Aquatic Microbial Metaproteomics Workflow: From Cells to Tryptic Peptides Suitable for Tandem Mass Spectrometry-based Analysis

Published on: September 15, 2015

9.2K
Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS
17:12

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS

Published on: December 20, 2010

16.0K

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Genetics

Background:

  • Selenoproteins incorporate selenocysteine (Sec), a noncanonical amino acid, via a unique UGA stop codon recoding mechanism involving the SECIS element.
  • Metazoans exhibit diverse selenoproteomes, with selenoproteins playing critical roles in redox homeostasis, signaling, and thyroid hormone metabolism.
  • Some animal lineages have lost the Sec pathway entirely, highlighting evolutionary divergence.

Purpose of the Study:

  • To summarize the molecular biology of Sec biosynthesis, metabolism, insertion, and regulation.
  • To examine the evolutionary dynamics of selenoproteins across metazoa, including gene duplications, losses, and Sec-to-cysteine substitutions.
  • To provide an updated survey of metazoan selenoprotein families, detailing their structure, function, and phylogenetic distribution.

Main Methods:

  • Literature review and synthesis of existing research on selenoprotein biology and evolution.
  • Comparative analysis of selenoprotein gene families across metazoan lineages.
  • Phylogenetic analysis to trace the evolutionary history of selenoproteins.

Main Results:

  • Detailed overview of Sec biosynthesis, co-translational insertion, and regulatory mechanisms.
  • Identification of diverse evolutionary trajectories, including gene duplication, loss, and amino acid substitution events in selenoprotein evolution.
  • Updated catalog of metazoan selenoprotein families with functional and phylogenetic data.

Conclusions:

  • Selenoprotein evolution is characterized by significant diversity across metazoa, with varying conservation and functional roles.
  • Understanding selenoprotein evolution provides insights into the adaptation and diversification of biological processes in animals.
  • This work offers a comprehensive resource for studying selenoprotein function and evolution in the animal kingdom.