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Related Concept Videos

Protein Networks02:26

Protein Networks

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,...
Protein Networks02:26

Protein Networks

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,...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Adaptability of Cytoskeletal Filaments01:12

Adaptability of Cytoskeletal Filaments

The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
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...

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JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
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JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

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Co-evolution and co-adaptation in protein networks.

David Juan1, Florencio Pazos, Alfonso Valencia

  • 1Structural Bioinformatics Group, Spanish National Cancer Research Centre (CNIO), C/Melchor Fernández Almagro 3, 28029 Madrid, Spain.

FEBS Letters
|February 20, 2008
PubMed
Summary

Protein families with similar evolutionary histories suggest co-adaptation or shared cellular processes. Current evidence supports both hypotheses influencing protein phylogenetic tree similarity.

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Bioinformatics

Background:

  • Proteins that interact or are functionally related often exhibit similar phylogenetic trees.
  • This observation has led to two primary hypotheses: co-adaptation and shared cellular processes.
  • Existing data support both explanations, suggesting a complex evolutionary interplay.

Purpose of the Study:

  • To explore the reasons behind the similarity in phylogenetic trees of functionally related proteins.
  • To evaluate the validity of co-adaptation versus shared cellular processes hypotheses.
  • To reconcile the current understanding of evolutionary pressures on protein families.

Main Methods:

  • Comparative analysis of phylogenetic trees for protein families.
  • Literature review of existing studies on protein evolution and function.
  • Bioinformatic approaches to assess evolutionary pressures and sequence similarities.

Main Results:

  • Phylogenetic tree similarity is a recurring observation in related protein families.
  • Evidence exists for compensatory evolutionary changes (co-adaptation) between protein families.
  • Functional relatedness and involvement in similar cellular processes also correlate with tree similarity.

Conclusions:

  • Both co-adaptation and shared evolutionary pressures from cellular processes contribute to similar phylogenetic trees.
  • The observed tree similarity is likely shaped by multiple evolutionary forces operating at different levels.
  • A comprehensive understanding requires considering both direct and indirect evolutionary influences.