Linked Life Data

3449857

Source:http://linkedlifedata.com/resource/pubmed/id/3449857

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-6-20
pubmed:abstractText
A second slow-cycling retinylidene protein, in addition to slow-cycling (sensory) rhodopsin (SR), can be bleached with hydroxylamine and regenerated with all-trans retinal in photosensory signaling Halobacterium halobium membranes. Flash photolysis shows this protein undergoes a photochemical reaction cycle characterized by photoconversion of its ground state (lambda max 480 nm) to a species with lambda max less than or equal to 360 nm, which thermally regenerates the 480-nm species with a t1/2 of 260 msec at 25 degrees C, under conditions in which SR photocycles at 650 msec in the same membranes. Mutants characterized with respect to their phototaxis behavior are identified which contain SR and the 480-nm pigment, the latter ranging from undetectable to a concentration equal to that of SR. Receptor mutants lacking all phototaxis sensitivity lack both of the photochemically reactive proteins. The mutant properties contribute to an accumulation of behavioral and spectroscopic evidence that the 480-nm pigment is a second sensory photoreceptor in H. halobium. NaDodSO4-polyacrylamide gel electrophoresis of [3H]retinal-labeled membrane proteins from the mutants indicates SR and the 480-nm pigment contain distinct chromophoric polypeptides differing in their migration rates. The data implicate polypeptides of 25,000 Mr and 23,000 Mr as retinal-binding polypeptides of SR and the 480-nm protein, respectively.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0887-3585
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
239-46
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Properties of a second sensory receptor protein in Halobacterium halobium phototaxis.
pubmed:affiliation
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't