Sensory rhodopsin II transducer HtrII is also responsible for serine chemotaxis in the archaeon Halobacterium salinarum.
Previously, we demonstrated that the methyl-accepting protein HtrII is the transducer for photoreceptor sensory rhodopsin II. Here, we provide experimental evidence that HtrII is also a chemotransducer. Using an agarose-in-plug bridge method, we show that an HtrII overexpression strain has a quicker response to serine than does an HtrII deletion strain. Furthermore, an in vivo flow assay demonstrates that the deletion strain is unable to modulate methylesterase activity after serine addition or photostimulation, while the overexpression strain shows distinct methanol peaks following both types of stimuli.
Hou
S
S
Department of Microbiology, University of Hawaii, Honolulu 96822, USA.
Brooun
A
A
Yu
H S
HS
Freitas
T
T
Alam
M
M
D019843:Archaeal Proteins; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D002265:Carboxylic Ester Hydrolases / Q000235:genetics / Q000378:metabolism; D002633:Chemotaxis / Q000235:genetics; D019641:DNA, Archaeal / Q000235:genetics; D019617:Halobacterium salinarum / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D000432:Methanol / Q000032:analysis / Q000378:metabolism; D017384:Sequence Deletion; D012694:Serine / Q000378:metabolism*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D019641:DNA, Archaeal; C100812:HtrII protein, Halobacterium salinarium; D012694:Serine; D002265:Carboxylic Ester Hydrolases; C041144:chemotactic protein methylesterase; D000432:Methanol