Assembling a protein-protein interaction map of the SSU processome from existing datasets
Young H Lim1, J Michael Charette, Susan J Baserga
1Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut, United States of America.
Plos One
|March 23, 2011
Summary
Protein-protein interactions within the small subunit (SSU) processome are largely unknown. Current data reveal sparse coverage of the SSU processome interactome, highlighting the need for further research into its assembly and function.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The small subunit (SSU) processome is crucial for ribosome biogenesis, comprising the U3 snoRNA and approximately 72 proteins.
- While SSU processome components are known, their protein-protein interactions (PPIs) and subsequent assembly, architecture, and function remain poorly understood.
Purpose of the Study:
- To assess the coverage of the SSU processome protein-protein interaction (PPI) network using existing high-throughput datasets.
- To identify gaps in knowledge regarding SSU processome protein interactions and guide future research.
Main Methods:
- Queried protein-protein interaction (PPI) databases for SSU processome proteins.
- Analyzed data from three genome-wide high-throughput yeast two-hybrid (HT-Y2H) studies, a genome-wide protein fragment complementation assay (PCA), and literature-curated (LC) datasets.
- Examined HT-Y2H datasets from six additional model organisms for conserved interactions.
Main Results:
- Coverage of the SSU processome PPI network is sparse across all analyzed datasets.
- The protein fragment complementation assay (PCA) dataset showed the highest coverage among genome-wide studies (27 PPIs, 25 proteins).
- Literature-curated (LC) data provided the most extensive interactome information (34 proteins, 38 PPIs), with many validated interactions.
- Over 70% of predicted PPIs remain undetermined, and 36% of proteins have no known interaction partners.
- Analysis of other model organisms yielded limited orthologous interactions.
Conclusions:
- Existing high-throughput methods provide incomplete coverage of the SSU processome interactome.
- A significant portion of SSU processome proteins lack identified interaction partners, hindering understanding of complex assembly and function.
- Further comprehensive genome-wide analyses, particularly yeast two-hybrid studies, are essential to elucidate the complete SSU processome interactome and its role in eukaryotic biology.
Related Concept Videos
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,...
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-protein Interfaces
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein 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...
Protein 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...


