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

Conservation of Protein Domains02:26

Conservation of Protein Domains

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conserved Binding Sites01:49

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 analyses the...
Conserved Binding Sites01:49

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 analyses the...
Evolutionary Relationships through Genome Comparisons02:54

Evolutionary Relationships through Genome Comparisons

Genome comparison is one of the excellent ways to interpret the evolutionary relationships between organisms. The basic principle of genome comparison is that if two species share a common feature, it is likely encoded by the DNA sequence conserved between both species. The advent of genome sequencing technologies in the late 20th century enabled scientists to understand the concept of conservation of domains between species and helped them to deduce evolutionary relationships across diverse...
Evolutionary Processes in Microbes01:26

Evolutionary Processes in Microbes

Microbial evolution occurs rapidly due to short generation times and a variety of genetic processes, including horizontal gene transfer, mutation, recombination, and genetic drift. These mechanisms collectively enable microbes to adapt swiftly to changing environments.Horizontal gene transfer (HGT) allows genes to move between different species and occurs through three main mechanisms: conjugation, transformation, and transduction. Conjugation involves direct cell-to-cell contact for DNA...

You might also read

Related Articles

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

Sort by
Same author

Codon bias shapes bacterial small RNA binding sites within protein-coding sequences.

RNA (New York, N.Y.)·2026
Same author

Formation of a membraneless compartment regulates bacterial virulence.

Nature communications·2025
Same author

Unraveling the interplay between a small RNA and RNase E in bacteria.

Nucleic acids research·2024
Same author

RIL-seq reveals extensive involvement of small RNAs in virulence and capsule regulation in hypervirulent Klebsiella pneumoniae.

Nucleic acids research·2024
Same author

Prolonged survival of a patient with active MDR-TB HIV co-morbidity: insights from a <i>Mycobacterium tuberculosis</i> strain with a unique genomic deletion.

Frontiers in medicine·2023
Same author

TRS: a method for determining transcript termini from RNAtag-seq sequencing data.

Nature communications·2023

Related Experiment Video

Updated: Jul 18, 2026

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Evolutionary conservation of domain-domain interactions.

Zohar Itzhaki1, Eyal Akiva, Yael Altuvia

  • 1Department of Molecular Genetics and Biotechnology, Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem 91120, Israel.

Genome Biology
|December 23, 2006
PubMed
Summary

Domain-domain interactions (DDIs) are key to understanding protein-protein interactions (PPIs). This study reveals conserved DDIs across species, acting as fundamental building blocks for cellular interactions.

More Related Videos

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
16:02

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation

Published on: February 10, 2023

Related Experiment Videos

Last Updated: Jul 18, 2026

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
16:02

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation

Published on: February 10, 2023

Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Evolutionary Biology

Background:

  • Investigating the relationship between domain-domain interactions (DDIs) and protein-protein interactions (PPIs) is crucial for understanding molecular mechanisms.
  • Recent research highlights the importance of DDIs in mediating PPIs.

Purpose of the Study:

  • To map structurally derived DDIs onto cellular PPI networks across diverse organisms.
  • To identify conserved domain pairs that serve as fundamental units for mediating protein interactions.

Main Methods:

  • Mapping of structurally derived DDIs onto PPI networks.
  • Comparative analysis of DDI repertoires in various species (E. coli, S. cerevisiae, C. elegans, D. melanogaster, H. sapiens).

Main Results:

  • A conserved catalog of domain pairs mediates diverse interactions within cellular PPI networks.
  • DDIs are prevalent in protein complexes, with abundant homotypic interactions.
  • Many DDIs are evolutionarily conserved across different organisms.

Conclusions:

  • Organisms utilize a common set of domain pairs as 'building blocks' for constructing PPIs.
  • The functional role of domain pairs in mediating protein interactions is evolutionarily conserved.