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Mycobacterium tuberculosis (Mtb) has successfully exploited macrophages as its primary niche in vivo. However, the bacterial requirements that promote its intracellular survival remain undefined. Our research interest is primarily organized to identify and unravel molecular mechanism of functioning of Mtb PhoP-PhoR system. Recent studies showing striking similarities between H37Ra and different Mtb phoP-phoR knock-out mutants in colony morphology, staining features and failure to grow as serpentine cords, led us to investigate whether MtbH37Ra expressed a functional PhoP-PhoR two-component system. As a beginning to understand the contribution of PhoP-PhoR system in Mtb physiology, a functional characterization of the phoP and phoR gene products was initiated in our laboratory. We investigate the origins of binding specificity in protein complexes, and probe the determinants of complex formation using biochemical assays. Our observations raise the possibility that PhoP may be capable of adopting different orientations as it binds to a vast array of genes to activate or repress transcription. Although much work remains to be done in identifying PhoP regulon in Mtb, our biochemical data on PhoP and its binding interactions(s) represents a significant advancement in beginning to understand the PhoPR system. Elucidation of the specific signal sensed by the Mtb PhoR sensor kinase is the next challenge to understand under which conditions and with which aim(s) PhoP function is regulated.
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