Claim · model-written summary
A 2-h-specific protein band of 13.5 kDa is found bound to thylakoid membranes after posttranslational transport.
- Taxon
- Barley
.jpg?width=60)
Hordeum vulgaret0 - Outcome
- 2-h-specific bandse5
- Value
- 13.5 kDae5
- Qualifier
- bound to thylakoid membranese5
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
.jpg?width=500)
Verbatim
e5“since after posttranslational transport 2-h-specific bands of 18.5 kDa, 18 kDa and 13.5 kDa have been found bound to thylakoid membranes”
t0“proteins of Barley”
Title
The early light‐inducible proteins of Barley °
Bernhard GRIMM; Klaus KLOPPSTECH European Journal of Biochemistry 1987. doi:10.1111/j.1432-1033.1987.tb13364.x
Other claims from this paper (11)
- Observation mRNAs of seven nuclear-coded proteins are transiently induced within 1-2 h of illumination of etiolated barley plants.
- Observation cDNA clones for early light-inducible proteins (ELIPs) were isolated.
- Observation The complete set of early light-inducible translation products is obtained with all investigated clones in hybrid-release translation.
- Observation Two ELIP families of high molecular mass (24-27 kDa) exist and are induced in parallel.
- Observation Two ELIP families of low molecular mass (16-18 kDa) exist and are induced in parallel.
- Observation Induction of ELIPs occurs even at very low light intensities.
- Observation Induction of ELIPs is saturated at about 1000 lx light intensity.
- Observation A 2-h-specific protein band of 18.5 kDa is found bound to thylakoid membranes after posttranslational transport.
- Observation A 2-h-specific protein band of 18 kDa is found bound to thylakoid membranes after posttranslational transport.
- Mechanism Some early light-inducible proteins are proposed to be precursors of chloroplast membrane proteins.
- Mechanism ELIPs are not considered light stress proteins but are considered to play a regulatory role during development.