Related Experiment Video
Updated: Dec 30, 2025
08:07
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
Published on: August 2, 2015
8.4K
Global discovery the PstP interactions using Mtb proteome microarray and revealing novel connections with EthR
Ke-Ke Li1, De-Hui Qu2, Hai-Nan Zhang3
1Key Laboratory of Molecular Module-Based Breeding of High Yield and Abiotic Resistant Plants in Universities of Shandong, School of Agriculture, Ludong University, Yantai 264025, China.
Journal of Proteomics
|January 21, 2020
Summary
This study identified 78 proteins interacting with Mycobacterium tuberculosis serine/threonine protein phosphatase PstP, revealing a novel link with EthR. PstP enhances EthR DNA binding, promoting ethionamide resistance in M. smegmatis.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Mycobacterium tuberculosis (Mtb) serine/threonine protein phosphatase PstP regulates cell division and growth via phosphorylation.
- The substrates and molecular mechanisms of PstP in Mtb remain largely unknown.
Purpose of the Study:
- To globally identify PstP binding partners in Mtb.
- To elucidate the functional role of PstP-interacting proteins, particularly EthR.
Main Methods:
- Mtb proteome microarray to identify PstP interactors.
- Bio-Layer interferometry and Yeast-two-hybrid assays for interaction validation.
- Functional studies on PstP-EthR interaction and its effect on DNA binding.
Main Results:
- Identified 78 Mtb proteins interacting with PstP.
- Validated a novel interaction between PstP and the transcription factor EthR.
- PstP enhances EthR binding to DNA, increasing ethionamide resistance in Mycobacterium smegmatis.
Conclusions:
- The identified PstP interactome provides a resource for understanding Mtb dephosphorylation pathways.
- The PstP-EthR interaction offers a potential target for novel tuberculosis drug development.
Related Concept Videos
02:26Protein Networks
4.4K
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,...
4.4K
01:33Proteomics
9.2K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
9.2K