The review covers recent progress on microbial sensory rhodopsins, vis
ual pigment-like retinylidene photoreceptors that function in phototax
is by archaeons, such as Halobacterium salinarium, and by unicellular
eukaryotic algae, such as Chlamydomonas reinhnrdtii. Six demonstrably
different sensory rhodopsins are known in halophilic archaea. The best
characterized is sensory rhodopsin I (SR-I), a color-sensitive recept
or that relays attractant and repellent photosignals to a tightly boun
d transducer protein HtrI (halobacterial transducer for sensory rhodop
sin I). New advances in the mechanism of signal transduction by the SR
-L/HtrI complex from molecular-biological and biophysical approaches a
re summarized. Effects of HtrI on light-induced proton transfers in th
e receptor are discussed for their possible role in signaling. Current
knowledge concerning the growing family of related archaeal sensory r
hodopsins is presented. The evidence for a sensory rhodopsin in photot
axis by C. reinhardtii and other unicellular eukaryotic algae is revie
wed. The molecular information is more limited than for the archaeal o
rganisms, but the physiological information is rich and complex. Compe
lling data exist for a single retinal-containing receptor mediating bo
th phototaxis and photophobic responses in C. reinhardtii. From retina
l analog studies, the isomeric configuration and ring/chain conformati
on of the retinal in the receptor appear to be identical to those of t
he archaeal sensory rhodopsins. Also, photoisomerization from all-tran
s- to 13-cis-retinal appears to be the trigger for signaling, as in th
e archaeal pigments. Conflicting early studies suggesting an 11-cis-re
tinal chromophore and signaling without photoisomerization are analyze
d and possible explanations for those reports are suggested. As a gene
ral conclusion, the microbial sensory rhodopsins provide an opportunit
y to explore photochemistry and protein/protein interaction in photose
nsory transduction in genetically tractable organisms.