6533b7d4fe1ef96bd1261db8
RESEARCH PRODUCT
The N-terminal domain of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for its acclimative proteolysis.
Dan-hui YangBertil AnderssonBertil AnderssonHarald Paulsensubject
Acclimative proteaseChlorophyll aN-terminal domainPhotosystem IImedicine.medical_treatmentProteolysisMutantMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsBiophysicsLight-Harvesting Protein ComplexesRecognition siteEndogenyLight-harvesting complex IIBiochemistrylaw.inventionchemistry.chemical_compoundStructural BiologylawSpinacia oleraceaGeneticsmedicineAmino Acid SequenceMolecular BiologyProteasemedicine.diagnostic_testSequence Homology Amino AcidChemistryBinding proteinHydrolysisPhotosystem II Protein ComplexCell BiologyBiochemistryRecombinant light-harvesting complex IIProteolysisRecombinant DNAdescription
AbstractVariations in the amount of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for regulation of the uptake of light into photosystem II. An endogenous proteolytic system was found to be involved in the degradation of LHCII in response to elevated light intensities and the proteolysis was shown to be under tight regulation [Yang, D.-H. et al. (1998) Plant Physiol. 118, 827–834]. In this study, the substrate specificity and recognition site towards the protease were examined using reconstituted wild-type and mutant recombinant LHCII. The results show that the LHCII apoprotein and the monomeric form of the holoprotein are targeted for proteolysis while the trimeric form is not. The N-terminal domain of LHCII was found to be essential for recognition by the regulatory protease and the involvement of the N-end rule pathway is discussed.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2000-01-25 | FEBS letters |