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Rhodopsin-Mediated Photoreception in Cryptophyte Flagellates
by
Sineshchekov, Oleg A.
, Govorunova, Elena G.
, Jung, Kwang-Hwan
, Maier, Uwe-G.
, Spudich, John L.
, Zauner, Stefan
in
Algae
/ Amino Acid Sequence
/ Aquatic plants
/ Cell Aggregation - radiation effects
/ Cell Biophysics
/ Chemicals
/ Chlamydomonas reinhardtii
/ Comparative analysis
/ Cryptomonas
/ Cryptophyta - physiology
/ Cryptophyta - radiation effects
/ Dose-Response Relationship, Radiation
/ E coli
/ Electric currents
/ Escherichia coli
/ Genes
/ Guillardia theta
/ Life sciences
/ Light
/ Molecular biology
/ Molecular Sequence Data
/ Photochemical reactions
/ Photochemicals
/ Photoreception
/ Photoreceptors, Microbial - physiology
/ Photoreceptors, Microbial - radiation effects
/ Proteins
/ Radiation Dosage
/ Rhodopsin - analysis
/ Rhodopsin - chemistry
/ Rhodopsin - metabolism
/ Sequence Homology, Amino Acid
/ Turnover time
/ Wavelengths
2005
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Rhodopsin-Mediated Photoreception in Cryptophyte Flagellates
by
Sineshchekov, Oleg A.
, Govorunova, Elena G.
, Jung, Kwang-Hwan
, Maier, Uwe-G.
, Spudich, John L.
, Zauner, Stefan
in
Algae
/ Amino Acid Sequence
/ Aquatic plants
/ Cell Aggregation - radiation effects
/ Cell Biophysics
/ Chemicals
/ Chlamydomonas reinhardtii
/ Comparative analysis
/ Cryptomonas
/ Cryptophyta - physiology
/ Cryptophyta - radiation effects
/ Dose-Response Relationship, Radiation
/ E coli
/ Electric currents
/ Escherichia coli
/ Genes
/ Guillardia theta
/ Life sciences
/ Light
/ Molecular biology
/ Molecular Sequence Data
/ Photochemical reactions
/ Photochemicals
/ Photoreception
/ Photoreceptors, Microbial - physiology
/ Photoreceptors, Microbial - radiation effects
/ Proteins
/ Radiation Dosage
/ Rhodopsin - analysis
/ Rhodopsin - chemistry
/ Rhodopsin - metabolism
/ Sequence Homology, Amino Acid
/ Turnover time
/ Wavelengths
2005
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Rhodopsin-Mediated Photoreception in Cryptophyte Flagellates
by
Sineshchekov, Oleg A.
, Govorunova, Elena G.
, Jung, Kwang-Hwan
, Maier, Uwe-G.
, Spudich, John L.
, Zauner, Stefan
in
Algae
/ Amino Acid Sequence
/ Aquatic plants
/ Cell Aggregation - radiation effects
/ Cell Biophysics
/ Chemicals
/ Chlamydomonas reinhardtii
/ Comparative analysis
/ Cryptomonas
/ Cryptophyta - physiology
/ Cryptophyta - radiation effects
/ Dose-Response Relationship, Radiation
/ E coli
/ Electric currents
/ Escherichia coli
/ Genes
/ Guillardia theta
/ Life sciences
/ Light
/ Molecular biology
/ Molecular Sequence Data
/ Photochemical reactions
/ Photochemicals
/ Photoreception
/ Photoreceptors, Microbial - physiology
/ Photoreceptors, Microbial - radiation effects
/ Proteins
/ Radiation Dosage
/ Rhodopsin - analysis
/ Rhodopsin - chemistry
/ Rhodopsin - metabolism
/ Sequence Homology, Amino Acid
/ Turnover time
/ Wavelengths
2005
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Rhodopsin-Mediated Photoreception in Cryptophyte Flagellates
Journal Article
Rhodopsin-Mediated Photoreception in Cryptophyte Flagellates
2005
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Overview
We show that phototaxis in cryptophytes is likely mediated by a two-rhodopsin-based photosensory mechanism similar to that recently demonstrated in the green alga
Chlamydomonas reinhardtii, and for the first time, to our knowledge, report spectroscopic and charge movement properties of cryptophyte algal rhodopsins. The marine cryptophyte
Guillardia theta exhibits positive phototaxis with maximum sensitivity at 450
nm and a secondary band above 500
nm. Variability of the relative sensitivities at these wavelengths and light-dependent inhibition of phototaxis in both bands by hydroxylamine suggest the involvement of two rhodopsin photoreceptors. In the related freshwater cryptophyte
Cryptomonas sp. two photoreceptor currents similar to those mediated by the two sensory rhodopsins in green algae were recorded. Two cDNA sequences from
G. theta and one from
Cryptomonas encoding proteins homologous to type 1 opsins were identified. The photochemical reaction cycle of one
Escherichia-coli-expressed rhodopsin from
G. theta (
GtR1) involves K-, M-, and O-like intermediates with relatively slow (∼80
ms) turnover time.
GtR1 shows lack of light-driven proton pumping activity in
E. coli cells, although carboxylated residues are at the positions of the Schiff base proton acceptor and donor as in proton pumping rhodopsins. The absorption spectrum, corresponding to the long-wavelength band of phototaxis sensitivity, makes this pigment a candidate for one of the
G. theta sensory rhodopsins. A second rhodopsin from
G. theta (
GtR2) and the one from
Cryptomonas have noncarboxylated residues at the donor position as in known sensory rhodopsins.
Publisher
Elsevier Inc,Biophysical Society
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