A proteome-wide protein interaction map for Campylobacter jejuni
Jodi R Parrish1, Jingkai Yu, Guozhen Liu
1Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Genome Biology
|July 7, 2007
Summary
This study systematically identified protein interactions for Campylobacter jejuni, a common food-borne pathogen. The resulting comprehensive interactome map aids in understanding bacterial functions and identifying potential antimicrobial drug targets.
Area of Science:
- Microbiology
- Systems Biology
- Proteomics
Background:
- Large-scale protein interaction data is crucial for systems biology, but limited for prokaryotes.
- Campylobacter jejuni is a significant food-borne pathogen causing widespread gastroenteritis.
- This study addresses the scarcity of prokaryotic protein interaction data.
Purpose of the Study:
- To systematically identify protein-protein interactions in Campylobacter jejuni.
- To create a comprehensive protein interaction map for C. jejuni.
- To leverage this map for functional predictions and identifying drug targets.
Main Methods:
- High-throughput yeast two-hybrid screens were employed for interaction detection.
- 11,687 protein interactions were detected and reproduced.
- The study covered 80% of predicted C. jejuni NCTC11168 proteins.
Main Results:
- A comprehensive C. jejuni protein interaction map was generated, integrating poorly characterized proteins into functional networks.
- Conserved subnetworks were identified by comparing C. jejuni networks with those of E. coli and S. cerevisiae.
- The map facilitated the identification of the C. jejuni chemotaxis pathway and a subnetwork of putative essential genes.
Conclusions:
- The C. jejuni protein interaction map is one of the most extensive for a free-living organism, nearly doubling available prokaryotic binary interactions.
- High coverage enables pathway mapping and function prediction for C. jejuni and orthologous proteins.
- The map supports cross-species comparisons to identify conserved protein interaction subnetworks and potential antimicrobial targets.
Related Concept Videos
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,...
01:26Bacterial Translocation and Protein Secretion
Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
02:04Protein-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...
02:04Protein-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...
01:25cAMP-dependent Protein Kinase Pathways
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...