Related Experiment Video
Updated: Jun 11, 2026

09:37
An Integrated Approach for Microprotein Identification and Sequence Analysis
Published on: July 12, 2022
Orthology confers intron position conservation.
Anna Henricson1, Kristoffer Forslund, Erik L L Sonnhammer
1Department of Cell and Molecular Biology, Karolinska Institutet, SE-17177 Stockholm, Sweden.
BMC Genomics
|July 6, 2010
Summary
Orthologous genes show higher intron position conservation than non-orthologs. This conserved intron position (IPC) score aids in accurately assigning gene orthology, improving evolutionary relationship analysis.
Area of Science:
- Genomics
- Evolutionary Biology
- Bioinformatics
Background:
- Accurate gene orthology assignment is crucial for functional inference from genomic data.
- Intron positions are conserved over evolutionary timescales, offering potential phylogenetic discriminating features.
- Investigating intron position conservation (IPC) can enhance orthology detection.
Purpose of the Study:
- To assess if orthologs exhibit higher intron position conservation (IPC) than non-orthologous sequences.
- To develop and validate a novel IPC scoring method for orthology assignment.
Main Methods:
- Developed a new IPC scoring system.
- Applied the IPC score to ortholog groups across human and six other species.
- Compared IPC scores between orthologous pairs and their closest non-orthologous counterparts.
Main Results:
- Orthologous gene pairs demonstrated significantly higher IPC than ortholog-non-ortholog pairs.
- Inparalog pairs also showed higher IPC than inparalog-non-inparalog pairs.
- High agreement was observed between IPC scores and the InParanoid algorithm's ortholog scores, with discordant cases highlighting links to multicellularity functions.
Conclusions:
- Orthologous genes exhibit greater conservation in intron positions compared to non-orthologous genes.
- The developed IPC score serves as a valuable supplementary metric for improving the accuracy of orthology assignment.
Related Concept Videos
Multi-species Conserved Sequences
Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale studies have provided new insights into the evolutionary relationship between organisms.
Although the genome of each species varies greatly from each other, a few sequences are highly conserved. Such conserved DNA...
Although the genome of each species varies greatly from each other, a few sequences are highly conserved. Such conserved DNA...
Synteny and Evolution
John H. Renwick first coined the term “synteny” in 1971, which refers to the genes present on the same chromosomes, even if they are not genetically linked. The species with common ancestry tend to show conserved syntenic regions. Therefore, the concept of synteny is nowadays used to describe the evolutionary relationship between species.
Around 80 million years ago, the human and mice lineages diverged from the common ancestor. During the course of evolution, the ancestral chromosome underwent...
Around 80 million years ago, the human and mice lineages diverged from the common ancestor. During the course of evolution, the ancestral chromosome underwent...
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...
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 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...
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...
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...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
LTR Retrotransposons
LTR retrotransposons are class I transposable elements with long terminal repeats flanking an internal coding region. These elements are less abundant in mammals compared to other class I transposable elements. About 8 percent of human genomic DNA comprises LTR retrotransposons. Some of the common examples of LTR retrotransposons are Ty elements in yeast and Copia elements in Drosophila.
The internal coding region of LTR retrotransposons and their mechanism of transposition closely resembles a...
The internal coding region of LTR retrotransposons and their mechanism of transposition closely resembles a...
