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Bacteria have devised phosphotransfer signaling mechanisms for eliciting a variety of adaptive responses to their environment. These mechanisms are collectively referred to as two-component regulatory systems. Each system generally consists of a sensor protein histidine kinase, which is anchored in the cell membrane, and a cytoplasmic response regulator, whose activity is modulated by the sensor. Most response regulators are transcription factors. In this review, we briefly introduce the established concept on bacterial two-component regulatory systems, using the Agrobacterium VirA-VirG system as an example, and give the evidence for the existence of quite similar systems in higher plants, such as the signal transduction induced by the phytohormone cytokinin. The Arabidopsis CRE1 histidine kinase and its related proteins AHK2 and AHK3 perceive cytokinins in the environment and transduce a signal, presumably through the AHP bridge components that carry the histidine-containing phosphotransfer (HPt) domain, to the ARR1 response regulator that transcriptionally activates genes immediately responsive to cytokinins. In addition, this signal transfer process appears to participate in cross-talk with signaling systems that respond to daylight and another phytohormone, ethylene, through an intracellular pool of several ARR1-like molecular species and the AHP components.

His-Asp phosphorelay signal transduction in higher plants: Receptors and response regulators for cytokinin signaling in Arabidopsis thaliana.