|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
10
|
|
pubmed:dateCreated |
1997-6-5
|
|
pubmed:abstractText |
Sensory rhodopsin II (SRII) is a repellent phototaxis receptor in the archaeon Halobacterium salinarum, similar to visual pigments in its seven-helix structure and linkage of retinal to the protein by a protonated Schiff base in helix G. Asp-73 in helix C is shown by spectroscopic analysis to be a counterion to the protonated Schiff base in the unphotolyzed SRII and to be the proton acceptor from the Schiff base during photoconversion to the receptor signaling state. Coexpression of the genes encoding mutated SRII with Asn substituted for Asp-73 (D73N) and the SRII transducer HtrII in H. salinarum cells results in a 3-fold higher swimming reversal frequency accompanied by demethylation of HtrII in the dark, showing that D73N SRII produces repellent signals in its unphotostimulated state. Analogous constitutive signaling has been shown to be produced by the similar neutral residue substitution of the Schiff base counterion and proton acceptor Glu-113 in human rod rhodopsin. The interpretation for both seven-helix receptors is that light activation of the wild-type protein is caused primarily by photoisomerization-induced transfer of the Schiff base proton on helix G to its primary carboxylate counterion on helix C. Therefore receptor activation by helix C-G salt-bridge disruption in the photoactive site is a general mechanism in retinylidene proteins spanning the vast evolutionary distance between archaea and humans.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-1356370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-1465418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-1867724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-1931988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-2252905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-2332402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-2682623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-2721495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-2808377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-2851326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-3410829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-3449857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-3767969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-6307914,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-7612849,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-7662864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-7777054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-7819500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-7833020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-7937859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-7961454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8001113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8180184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8224146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8636990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8639619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8643458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8710852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8746630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8791445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8800472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9144172-8898094
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
13
|
|
pubmed:volume |
94
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
4960-5
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:9144172-Amino Acid Sequence,
pubmed-meshheading:9144172-Archaeal Proteins,
pubmed-meshheading:9144172-Aspartic Acid,
pubmed-meshheading:9144172-Bacteriorhodopsins,
pubmed-meshheading:9144172-Binding Sites,
pubmed-meshheading:9144172-Carotenoids,
pubmed-meshheading:9144172-Cell Movement,
pubmed-meshheading:9144172-Darkness,
pubmed-meshheading:9144172-Halobacterium,
pubmed-meshheading:9144172-Halorhodopsins,
pubmed-meshheading:9144172-Humans,
pubmed-meshheading:9144172-Kinetics,
pubmed-meshheading:9144172-Light,
pubmed-meshheading:9144172-Molecular Sequence Data,
pubmed-meshheading:9144172-Mutagenesis, Site-Directed,
pubmed-meshheading:9144172-Point Mutation,
pubmed-meshheading:9144172-Protein Structure, Secondary,
pubmed-meshheading:9144172-Recombinant Proteins,
pubmed-meshheading:9144172-Schiff Bases,
pubmed-meshheading:9144172-Sensory Rhodopsins,
pubmed-meshheading:9144172-Signal Transduction,
pubmed-meshheading:9144172-Spectrophotometry
|
|
pubmed:year |
1997
|
|
pubmed:articleTitle |
Constitutive signaling by the phototaxis receptor sensory rhodopsin II from disruption of its protonated Schiff base-Asp-73 interhelical salt bridge.
|
|
pubmed:affiliation |
Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, TX 77030, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
