Oxygen affinities of DosT and DosS sensor kinases with implications for hypoxia adaptation in Mycobacterium tuberculosis.

DosT and DosS are heme-based kinases involved in sensing and signaling O tension in the microenvironment of Mycobacterium tuberculosis (Mtb). Under conditions of low O, they activate >50 dormancy-related genes and play a pivotal role in the induction of dormancy and associated drug resistance during tuberculosis infection. In this work, we reexamine the O binding affinities of DosT and DosS to show that their equilibrium dissociation constants are 3.

Oxygen affinities of DosT and DosS sensor kinases with implications for hypoxia adaptation in .

DosT and DosS are heme-based kinases involved in sensing and signaling O tension in the microenvironment of (). Under conditions of low O, they activate >50 dormancy-related genes and play a pivotal role in the induction of dormancy and associated drug resistance during tuberculosis infection. In this work, we reexamine the O binding affinities of DosT and DosS to show that their equilibrium dissociation constants are 3.

Metalloprotein enabled redox signal transduction in microbes.

Microbes utilize numerous metal cofactor-containing proteins to recognize and respond to constantly fluctuating redox stresses in their environment. Gaining an understanding of how these metalloproteins sense redox events, and how they communicate such information downstream to DNA to modulate microbial metabolism, is a topic of great interest to both chemists and biologists. In this article, we review recently characterized examples of metalloprotein sensors, focusing on the coordination and oxidation state of the metals involved, how these metals are able to recognize redox stimuli, and how the signal is transmitted beyond the metal center.