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Abstract
Phosphotransfer-mediated signaling pathways allow cells to sense and respond to environmental
stimuli. Autophosphorylating histidine protein kinases provide phosphoryl groups for
response regulator proteins which, in turn, function as molecular switches that control
diverse effector activities. Structural studies of proteins involved in two-component
signaling systems have revealed a modular architecture with versatile conserved domains
that are readily adapted to the specific needs of individual systems.