Component of the Rhodospirillum centenum photosensory apparatus with structural and functional similarity to methyl-accepting chemotaxis protein chemoreceptors
Zy. Jiang et Ce. Bauer, Component of the Rhodospirillum centenum photosensory apparatus with structural and functional similarity to methyl-accepting chemotaxis protein chemoreceptors, J BACT, 183(1), 2001, pp. 171-177
Photosynthetic bacteria respond to alterations in light conditions by migra
ting to locations that allows optimal use of light as an energy source. Stu
dies have indicated that photosynthesis-driven electron transport functions
as an attractant signal for motility among purple photosynthetic bacteria,
However, it is unclear just how the motility-based signal transduction sys
tem monitors electron how through photosynthesis-driven electron transport.
Recently, we have demonstrated that the purple photosynthetic bacterium Rh
odospirillum centenum is capable of rapidly moving swarm cell colonies towa
rd infrared light as well as away from visible light. Light-driven colony m
otility of R. centenum has allowed us to perform genetic dissection of the
signaling pathway that affects photosynthesis-driven motility, In this stud
y, we have undertaken sequence and mutational analyses of one of the compon
ents of a signal transduction pathway, Ptr, which appears responsible for t
ransmitting a signal from the photosynthesis-driven electron transport chai
n to the chemotaxis signal transduction cascade. Mutational analysis demons
trates that cells disrupted for ptr are defective in altering motility in r
esponse to light, as well as defective in light-dependent release of methan
ol. We present a model which proposes that Ptr senses the redox state of a
component in the photosynthetic cyclic electron transport chain and that Pt
r is responsible for transmitting a signal to the chemotaxis machinery to i
nduce a photosynthesis-dependent motility response.