Related Experiment Video
Updated: May 27, 2026
11:12
Identification of protein complexes with quantitative proteomics in S. cerevisiae
Published on: March 4, 2009
Correlation of disorder between S. cerevisiae interacting proteins
Kevin Rue-Albrecht1, Denis C Shields, Nora Khaldi
1UCD Conway Institute of Biomolecular and Biomedical Research, School of Medicine and Medical Sciences, University College Dublin, Dublin, Republic of Ireland. kevin.rue@ucdconnect.ie
Molecular Biosystems
|November 24, 2011
Summary
Protein disorder levels correlate between interacting proteins, especially within complexes. This suggests coordinated evolution and highlights the importance of similar disorder in complex subunits for network stability.
Area of Science:
- Molecular Biology
- Bioinformatics
- Evolutionary Biology
Background:
- Protein disorder is linked to protein-protein interactions.
- The evolution of protein disorder within interaction networks is not well understood.
- Coordinated evolution of interacting proteins is observed in evolutionary rates and gene expression.
Purpose of the Study:
- To investigate the relationship between the disorder levels of interacting proteins.
- To compare disorder correlations in binary versus complex protein interactions.
- To understand how protein disorder evolves within protein-protein interaction networks.
Main Methods:
- Analysis of predicted disorder residues in binary and complex interacting proteins.
- Examination of disorder correlations between interacting protein partners.
- Comparison of disorder variation across different types of protein complexes.
Main Results:
- Interacting proteins show correlated levels of disorder.
- Higher disorder correlation is observed in proteins within the same complex compared to binary interactors.
- Significant variation in disorder levels exists within complexes, particularly in RNA processes and protein binding complexes.
Conclusions:
- Co-members of protein complexes likely experience stronger selection for similar disorder than binary interactors.
- Complex interactions may be more sensitive to changes in protein disorder than binary interactions.
- Maintaining similar disorder levels among complex subunits is crucial for protein network function and stability.
Related Concept Videos
01:28Yeast Signaling
Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
02:26Protein 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,...
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,...
02:26Protein 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,...
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,...
02:18Intrinsically Disordered Proteins
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
02:18Intrinsically Disordered Proteins
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
01:57Protein 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 to...
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 to...