Abstract

TERAN-MELO, Juan Luis; RODRIGUEZ-RANGEL, Claudia; GEORGELLIS, Dimitris  and  ALVAREZ, Adrián F.. Autophosphorylation and transphosphorylation mechanisms in bacterial two component systems. TIP [online]. 2019, vol.22, e162.  Epub Mar 04, 2020. ISSN 1405-888X.  https://doi.org/10.22201/fesz.23958723e.2018.0.162.

Two-component signaling circuits (TCS) allow bacteria to detect environmental cues and to produce adaptive responses. These signaling systems are based on autophosphorylation and phosphoryl-group transfers between histidine and aspartate containing sensor kinase and response regulator proteins. Upon reception of a specific stimulus the sensor kinase protein autophosphorylates, by either an inter- or intra-molecular reaction, and transphosphorylates its cognate response regulator, which, typically, acts as a transcriptional regulator, thereby triggering physiological responses. Frequently, in the absence of the stimulus, the sensor kinase proteins are responsible for the dephosphorylation of their cognate response regulators. Furthermore, a group of sensor kinases have additional functional domains that are involved in a forward phosphorelay for signal transmission and in a reverse phosphorelay for signal decay. As is the case of the autophosphorylation reaction, the phosphoryl-group transfers involved in the forward and reverse phosphorelay can occur either intra- or inter-molecularly. In this review, we highlight some important features of bacterial TCS, with special emphasis on the autophosphorylation and phosphoryl-group transfer events.

Keywords : sensor kinase; autophosphorylation; transphosphorylation; intermolecular; intramolecular.

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