Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Diversity of Archaea IV

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...

Diversity of Archaea III

Diversity of Archaea III

Crenarchaeota, a prominent phylum of Archaea, is remarkable for its ability to thrive in extreme environments characterized by high temperatures and acidity. These microorganisms inhabit sulfuric hot springs, volcanic systems, and submarine hydrothermal vents, where temperatures often exceed 100°C. The unique adaptations of Crenarchaeota not only allow survival under such extreme conditions but also provide insights into the mechanisms of life in primordial Earth-like...

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

Gene Evolution - Fast or Slow?

Gene Evolution - Fast or Slow?

The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
In contrast, regions which code...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...

Allosteric Proteins-ATCase

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...

You might also read

Related Articles

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

Sort by

Same author

Substrate scope of ancestral versus modern family-1 glycosidases.

Protein science : a publication of the Protein Society·2026

Same author

Human Transglutaminases: Updated Insights into Activation Mechanisms, Allosteric Regulation and Disease.

International journal of molecular sciences·2026

Same author

Molecular analysis of 3D domain swapping in the acylphosphatase from Escherichia coli.

Acta crystallographica. Section D, Structural biology·2026

Same author

An enzymatic microfluidic sensor for β-lactam antibiotics based on cross-linked ancestral β-lactamase crystals.

Nanoscale advances·2026

Same author

Conformational Dynamics and Catalytic Backups in a Hyper-thermostable Engineered Archaeal Protein Tyrosine Phosphatase.

JACS Au·2026

Same author

New human bisphosphoglycerate mutase structures provide insights into the structural basis of BPGM deficiency and citrate inhibition.

International journal of biological macromolecules·2025

Search research articles

Related Experiment Video

Updated: Mar 16, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Engineering ancestral protein hyperstability.

M Luisa Romero-Romero¹, Valeria A Risso¹, Sergio Martinez-Rodriguez¹

¹Departamento de Quimica Fisica, Facultad de Ciencias, Universidad de Granada, Campus Fuentenueva s/n, Granada 18071, Spain.

The Biochemical Journal

|August 17, 2016

Summary

This summary is machine-generated.

Engineered ancestral proteins show enhanced stability. Comparing resurrected ancestral proteins identified mutations increasing thermostability, offering a simple method for discovering extreme protein properties.

Keywords:

protein engineering protein stability resurrected proteins thioredoxin

More Related Videos

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Related Experiment Videos

Last Updated: Mar 16, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Area of Science:

Biochemistry
Molecular Evolution
Protein Engineering

Background:

Ancient life is hypothesized to be thermophilic.
Reconstructed ancestral proteins often exhibit high stability.

Purpose of the Study:

To engineer enhanced stability in reconstructed ancestral proteins.
To develop a straightforward method using ancestral reconstruction information.

Main Methods:

Resurrected a thioredoxin from the last common ancestor of cyanobacterial, Deinococcus, and Thermus groups (LPBCA thioredoxin).
Screened mutations between evolutionarily related resurrected ancestral proteins.
Experimentally compared LPBCA thioredoxin with a resurrected thioredoxin from the last common ancestor of bacteria.

Main Results:

LPBCA thioredoxin demonstrated a denaturation temperature of ~123°C.
Identified three mutations that increased LPBCA thioredoxin's denaturation temperature to ~128°C.
This approach expands ancestral reconstruction for discovering extreme protein properties.

Conclusions:

Comparing evolutionarily related resurrected ancestral proteins is a simple approach to enhance protein stability.
This method can identify mutations for extreme protein properties with biotechnological potential.
Ancestral sequence derivation from modern sequences ensures broad applicability.