The Treponema denticola PAS Domain-Containing Histidine Kinase Hpk2 Is a Heme Binding Sensor of Oxygen Levels.

摘要: Periodontal disease (PD) results from a shift in the composition of microbial community subgingival crevice. As bacterial population transitions Gram-positive bacteria to predominantly Gram-negative anaerobes and spirochetes, dramatic changes occur physiological immunological environment at diseased sites. Treponema denticola thrives periodontal pockets, indicating that it has unique ability adapt changing environmental conditions. Hpk2 (tde1970), Per-Arnt-Sim motif (PAS) domain-containing histidine kinase (HK), is part T. Hpk2-Rrp2 (tde1969) two-component regulatory (TCR) system. This TCR system growth phase regulated been postulated play key role adaptive responses. In this study, we employ predictive structural analyses site-directed mutagenesis investigate functional specific amino acid residues located within PAS domain. Specific substitutions impacted autophosphorylation (AP), phosphotransfer (PT), oligomerization, hemin binding. The AP, PT, binding, oligomerization potential some mutated proteins differed under aerobic versus anaerobic reaction data presented here suggest activity linked diatomic gas levels. broader sense, study highlights importance studying produced by conditions approximate which they thrive.IMPORTANCE affects nearly 60% global adult population. Its costs individuals, society as whole, are enormous. develops, there oral community. become dominant able cause significant damage tissues support teeth, leading tooth loss. one keystone pathogens associated with disease. An earlier demonstrated Rrp2 an important Here, explore acids sensing function, using mutagenesis.