rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1990-6-29
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pubmed:abstractText |
An analogue of all-trans retinal in which all-trans/13-cis isomerization is blocked by a carbon bridge from C12 to C14 was incorporated into the apoproteins of sensory rhodopsin I (SR-I) and sensory rhodopsin II (SR-II, also called phoborhodopsin) in retinal-deficient Halobacterium halobium membranes. The "all-trans-locked" retinal analogue forms SR-I and SR-II analogue pigments with similar absorption spectra as the native pigments. Blocking isomerization prevents the formation of the long-lived intermediate of the SR-I photocycle (S373) and those of the SR-II photocycle (S-II360 and S-II530). A computerized cell tracking and motion analysis system capable of detecting 2% of native pigment activity was used for assessing motility behavior. Introduction of the locked analogue into SR-I or SR-II apoprotein in vivo did not restore phototactic responses through any of the three known photosensory systems (SR-I attractant, SR-I repellent, or SR-II repellent). We conclude that unlike the phototaxis receptor of Chlamydomonas reinhardtii, which has been reported to mediate physiological responses without specific double-bond isomerization of its retinal chromophore (Foster et al., 1989), all-trans/13-cis isomerization is essential for SR-I and SR-II phototaxis signaling.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-1161001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-15874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-16590155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-19246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-19431594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-2424472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-2713348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-2985136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-2988577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-3191096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-3293584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-3372482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-3427042,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-3449857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-3790692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-3977930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-4016190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-4084506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-4876934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-5474532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-6098298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-6281770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-6287921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-6493336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-6504161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-6959114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-7020578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-7074022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-7243905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-7272450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-728405,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-7387982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-7466366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-870032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2344465-915165
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-3495
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
807-14
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:2344465-Archaeal Proteins,
pubmed-meshheading:2344465-Bacteriorhodopsins,
pubmed-meshheading:2344465-Carotenoids,
pubmed-meshheading:2344465-Cell Movement,
pubmed-meshheading:2344465-Halobacterium,
pubmed-meshheading:2344465-Halorhodopsins,
pubmed-meshheading:2344465-Isomerism,
pubmed-meshheading:2344465-Kinetics,
pubmed-meshheading:2344465-Light,
pubmed-meshheading:2344465-Photochemistry,
pubmed-meshheading:2344465-Retinaldehyde,
pubmed-meshheading:2344465-Retinoids,
pubmed-meshheading:2344465-Sensory Rhodopsins,
pubmed-meshheading:2344465-Signal Transduction,
pubmed-meshheading:2344465-Spectrophotometry
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pubmed:year |
1990
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pubmed:articleTitle |
All-trans/13-cis isomerization of retinal is required for phototaxis signaling by sensory rhodopsins in Halobacterium halobium.
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pubmed:affiliation |
Department of Chemistry, Columbia University, New York 10027.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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