Devendra Pratap Singh

The paper identifies MutT1 as a phosphatase that dephosphorylates sensor kinases in Mycobacterium tuberculosis, revealing a new regulatory mechanism in two-component signaling.

This paper shows that mycobacterial MutT1, through its Nudix hydrolase domain, functions as a protein phosphatase to regulate NDK-Pi levels and prevent the conversion of 8-oxo-dGDP to 8-oxo-dGTP, thereby reducing A to C mutations.

The paper shows that non-cognate response regulators sequester phosphorylated histidine kinases, establishing a threshold for bacterial two-component signaling to prevent over-response to weak signals.

The paper identifies PdtaS as a c-di-GMP binding histidine kinase that regulates mycobacterial adaptation to nutrient deprivation through transcriptional and metabolic changes.