Related Experiment Video
Updated: May 22, 2026

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
Published on: January 11, 2017
Protein-protein interactions between histidine kinases and response regulators of Mycobacterium tuberculosis H37Rv
Ha-Na Lee1, Kwang-Eun Jung, In-Jeong Ko
1Department of Microbiology, Pusan National University, Busan, 609-735, Republic of Korea.
Abstract:
Using yeast two-hybrid assay, we investigated protein-protein interactions between all orthologous histidine kinase (HK)/response regulator (RR) pairs of M. tuberculosis H37Rv and identified potential protein-protein interactions between a noncognate HK/RR pair, DosT/NarL. The protein interaction between DosT and NarL was verified by phosphotransfer reaction from DosT to NarL. Furthermore, we found that the DosT and DosS HKs, which share considerable sequence similarities to each other and form a two-component system with the DosR RR, have different cross-interaction capabilities with NarL: DosT interacted with NarL, while DosS did not. The dimerization domains of DosT and DosS were shown to be sufficient to confer specificity for DosR, and the different cross-interaction abilities of DosS and DosT with NarL were demonstrated to be attributable to variations in the amino acid sequences of the α2-helices of their dimerization domains.
More Related Videos
Related Concept Videos
The JAK-STAT Signaling Pathway
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Other Stress Responses in Bacteria
Regulation of Bacterial Virulence
Protein-protein Interfaces
PI3K/mTOR/AKT Signaling Pathway

