Protein Receptors Evolved from Homologous Cohesion Modules That Self-Associated and Are Encoded by Interactive
1Departments of Psychiatry and Behavioral Medicine and Pharmacology, Toxicology and Neuroscience, LSU Health Shreveport, 1501 Kings Highway, Shreveport, LA 71130, USA.
Life (Basel, Switzerland)
|December 24, 2021
Summary
Protein receptors likely evolved from self-binding peptides encoded by dispersed gene segments. Receptor genes show extensive genomic interactions, suggesting evolutionary conservation and adaptive relocation for coordinated regulation.
Area of Science:
- Genomics
- Molecular Biology
- Evolutionary Biology
Background:
- Protein receptors are hypothesized to originate from self-binding peptides encoded by dispersed, self-interacting gene segments.
- Peptide self-association is thought to be driven by regions of amino acid similarity.
Purpose of the Study:
- To investigate the evolutionary origins and genomic dynamics of protein receptors.
- To explore special features of receptors, including homology and gene arrangement.
Main Methods:
- Utilized BLASTP searches to identify homologous proteins for receptor sequences compared to non-receptor proteins.
- Analyzed gene-gene interactions for a panel of receptor genes against randomly selected genes.
- Examined the genomic location of receptor genes for evidence of adaptive relocation.
Main Results:
- Receptor sequences yielded significantly more unique homologous protein hits than non-receptor sequences, supporting the duplication and dispersal of receptor building blocks (cohesion modules).
- Receptor genes were involved in a greater number of gene-gene interactions, indicating enhanced evolutionary conservation and network integration.
- Some receptor genes were found in regions of active gene relocation, suggesting potential for coordinated regulation and chromatin modification.
Conclusions:
- Findings support the model of receptor evolution from duplicated, dispersed gene segments with maintained structure/function relationships.
- The extensive genomic integration and adaptive relocation of receptor genes highlight their evolutionary importance and regulatory flexibility.
- Coordinated communication between receptors and their encoding genes is proposed as a key aspect of their function and evolution.
Keywords:
cohesion modulesgene interaction networksreceptor evolutionself-organizationsyntenic blocks of genesMore Related Videos
07:03Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
Published on: December 23, 2022
3.2K
07:57Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
Published on: August 21, 2019
8.6K
Related Concept Videos
01:30Assembly of Signaling Complexes
6.0K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.0K
02:04Covalently Linked Protein Regulators
1.8K
1.8K
01:49Conserved Binding Sites
4.6K
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...
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...
4.6K
01:57Protein Complexes with Interchangeable Parts
2.6K
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...
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...
2.6K
02:26Protein Networks
4.1K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.1K
01:15G Protein-coupled Receptors
13.9K
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
13.9K