A. Imamura et al., RESPONSE REGULATORS IMPLICATED IN HIS-TO-ASP PHOSPHOTRANSFER SIGNALING IN ARABIDOPSIS, Proceedings of the National Academy of Sciences of the United Statesof America, 95(5), 1998, pp. 2691-2696
The His to Asp phosphotransfer signal transduction mechanism involves
three common signaling domains: the transmitter (or His-kinase), the r
eceiver, and the histidine-containing phototransfer (HPt) domain, Typi
cally, a sensor kinase has a His-kinase domain and a response regulato
r has a receiver domain containing a phosphoaccepting aspartate, where
as a histidine-containing phototransfer domain serves as a mediator of
the histidine-to-aspartate phosphotransfer. This signal transduction
mechanism was thought to be restricted to prokaryotes. However, many e
xamples have been discovered in diverse eukaryotic species including h
igher plants, In Arabidopsis, three sensor kinases have been character
ized, namely, ETR1, ERS, and CKI1, which were suggested to be involved
in ethylene-and cytokinin-dependent signal transduction pathways, res
pectively. To date, no response regulator has been discovered in highe
r plants, We identify five distinct Arabidopsis response regulator gen
es, each encoding a protein containing a receiver-like domain, In vivo
and in vitro evidence that ARRs can function as phosphoaccepting resp
onse regulators was obtained by employing the Escherichia coil His-Asp
phosphotransfer signaling system.