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Bacterial signal transduction

Bacterial signal transduction systems are information processing pathways that link an environmental stimulus with an adaptive cellular response. Several signaling pathways have been experimentally demonstrated to control important cellular functions including metabolism, quorum sensing, chemotaxis, transport, respiration, development, osmoregulation, and many more (Stock et al., 2000). Additionally, signal transduction systems regulate virulence, host-recognition, and antibiotic resistance in major human pathogens including Staphylococcus aureus, Streptococcus penumonia, Streptococcus pyogenes, Vibrio cholerae, Mycobacterium tuberculosis, Clostridium difficile, and many more.

Common to all bacterial signal transduction systems is the detection of a signal (input) and coupling this with an adaptive cellular response (output); however, bacteria employ diverse mechanisms for linking these events, ranging from single-domain transducers to several interacting proteins. The simplest and most abundant signal transduction systems are one-component systems that possess both sensory and regulatory properties on a single protein molecule (Ulrich et al., 2005). The most widely recognized signaling systems are two-component systems that utilize protein phosphorylation as a fundamental strategy for signaling (Hoch and Silhavy, 1995; Stock et al., 2000; Inouye and Dutta, 2003). The prototypical two-component systems consists of a membrane-bound, sensor histidine kinase and a cytoplasmic response regulator. The sensor kinase detects an environmental signal via its input domain(s). This triggers an ATP-dependent autophosphorylation of a conserved histidine residue within its carboxy-terminal transmitter domain. The response regulator then catalyzes the transfer of this phosphoryl group to a conserved aspartate residue within its receiver domain. Phosphorylation of the receiver domain activates the output domain(s), which effects a particular adaptive response, usually regulation of transcription (Parkinson and Kofoid, 1992). Phosphorelays extends the basic two-component them with the inclusion of additional histidine phosphotransfer (HPt) and aspartate containing receiver domains (Appleby et al., 1996, Hoch, 2000).

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