The product of cbr, structurally similar to Elips (early light-induced proteins of higher plants)
First-pass extracted concept
Cbr
Candidate: toolkit item2 source documents14 linked claims
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Aliases
cbr gene product, cbr predicted product
Evidence Snippets
The predicted product of cbr is closely related to early light-induced proteins (Elips) of higher plants, and also shows resemblance to chlorophyll a/b-binding proteins.
Supporting Sources
Linked Claims
The authors propose that Cbr and early light-induced proteins bind zeaxanthin to form photoprotective complexes within light-harvesting antennae.
Quoted textsource-backed
Based on these results we propose that Cbr/early light-induced proteins bind zeaxanthin to form photoprotective complexes within the light-harvesting antennae.
After transfer from low to high light, zeaxanthin is associated with the faster migrating photosystem II light-harvesting complex fractions that also contain Cbr.
Quoted textsource-backed
In cells transferred from low to high light, zeaxanthin was associated with the faster migrating of two electrophoretically resolved fractions of light harvesting complexes of photosystem II that also contained Cbr.
When highly illuminated cells are returned to normal light, Cbr decays in parallel with reepoxidation of zeaxanthin to violaxanthin.
Quoted textsource-backed
When highly illuminated cells were returned to normal light, Cbr decayed in parallel to the reepoxidation of zeaxanthin to violaxanthin.
Cbr induction parallels violaxanthin deepoxidation to zeaxanthin under high light, sulfate starvation, or norflurazon treatment.
Quoted textsource-backed
A parallel between the two processes was observed in cells exposed to high light, starved for sulfate, or treated with norflurazon
Nondenaturing gel electrophoresis provided evidence for a physical association between Cbr and zeaxanthin.
Quoted textsource-backed
Evidence for the physical association of Cbr and zeaxanthin was provided by nondenaturing gel electrophoresis.
In Dunaliella bardawil, cbr is transcriptionally and translationally activated in parallel with accelerated carotenogenesis under light stress conditions.
Quoted textsource-backed
The cbr gene, previously cloned from the unicellular green alga Dunaliella bardawil, is transcriptionally and translationally activated in parallel to accelerated carotenogenesis in response to light stress conditions.
The Cbr product is structurally similar to plant early light-induced proteins.
Quoted textsource-backed
The product of cbr, structurally similar to Elips (early light-induced proteins of higher plants)
After mild solubilization, Cbr co-fractionated with light-harvesting complex II and was specifically associated with a minor LHCII complex.
Quoted textsource-backed
After mild solubilization, Cbr co-fractionated with light-harvesting complex II (LHCII) in sucrose gradient centrifugation and gel electrophoresis and was specifically associated with a minor LHCII complex.
The results support the conclusion that Cbr belongs to a class of stress-induced proteins transiently associated with antennae complexes.
Quoted textsource-backed
These results support the conclusion that Cbr belongs to a class of stress-induced proteins transiently associated with antennae complexes.
The anti-Cbr antibodies cross-reacted with an approximately 20-kDa polypeptide in sulfate-starved Dunaliella salina.
Quoted textsource-backed
The antibodies also cross-reacted with an approximately 20-kDa polypeptide in sulfate-starved Dunaliella salina.
The predicted product of cbr is closely related to early light-induced proteins of higher plants and resembles chlorophyll a/b-binding proteins.
Quoted textsource-backed
The predicted product of cbr is closely related to early light-induced proteins (Elips) of higher plants, and also shows resemblance to chlorophyll a/b-binding proteins.
Antibodies against a synthetic Cbr oligopeptide recognized two Cbr-associated polypeptides of approximately 17 and 19 kDa in Dunaliella bardawil.
Quoted textsource-backed
Antibodies raised against a synthetic oligopeptide matching the predicted sequence of Cbr recognized two polypeptides of apparently 17 and 19 kDa
Cbr polypeptides are induced in parallel with cbr transcript accumulation in highly illuminated or sulfate-starved Dunaliella bardawil cells.
Quoted textsource-backed
Antibodies raised against a synthetic oligopeptide matching the predicted sequence of Cbr recognized two polypeptides of apparently 17 and 19 kDa that were induced in parallel to cbr transcript accumulation in highly illuminated or sulfate-starved D. bardawil cells.
In both Dunaliella bardawil and Dunaliella salina, Cbr was found exclusively in thylakoid membranes.
Quoted textsource-backed
In both D. bardawil and D. salina, Cbr was found exclusively in the thylakoid membranes.