J. Rudolph et D. Oesterhelt, CHEMOTAXIS AND PHOTOTAXIS REQUIRE A CHEA HISTIDINE KINASE IN THE ARCHAEON HALOBACTERIUM-SALINARIUM, EMBO journal, 14(4), 1995, pp. 667-673
Histidine kinases are part of the two-component signal transduction sy
stem responsible for eubacterial responses to diverse environmental si
gnals, They have recently been detected in eukaryotes but their existe
nce in the kingdom Archaea remains uncertain, Here we report the seque
nce and function of a histidine kinase (CheA(H.s.)) from Halobacterium
salinarium, the first such transmitter in Archaea. The protein CheA(H
.s.) (668 residues) has significant sequence identity with the CheA pr
oteins known from eubacterial signal transduction (e.g, 34% identity w
ith CheA from Bacillus subtilis). Antibodies were raised against CheA(
H.s.), as expressed in Escherichia coli and were used in Western blott
ing to demonstrate the expression of cheA(H.s.) in H.salinarium. As ha
s been observed for other halophilic proteins, CheA(H.s.) has a devian
t electrophoretic migration, with an apparent molecular weight of 103
kDa on SDS-PAGE compared with a calculated molecular weight of 72 kDa,
Deletion of a part of the cheA(H.s.) gene leads to loss of both chemo
tactic and phototactic responses in H.salinarium as measured by swarm
plate assays, motion analysis and tethering experiments, This indicate
s that CheA(H.s.) plays a crucial role in chemical and light signal in
tegration, presumably interacting with at least two phototransducers a
nd a number of chemoreceptors.