Ser/Thr phosphorylation of <i>Mycobacterium tuberculosis</i> type II RelK toxin by PknK destabilizes TA interaction and interferes with toxin neutralization

Bacterial pathogens rely on the phenomenon of persistence as a survival strategy to combat the adverse environmental conditions encountered during infection. As a stochastic process, the driving force(s) that potentiate the formation of persisters in a bacterial population are largely unclear. This study is a step towards the discovery of intricate regulatory mechanisms that coordinate a synchronized TA cellular program. We propose a model where the TA module is regulated post-translationally, specifically via Ser/Thr phosphorylation disrupting the interaction between the toxin and antitoxin proteins as a mechanism to regulate TA function.