AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence

Degradation of the most abundant membrane protein on earth, the light-harvesting complex of Photosystem II (LHC II), is highly regulated under various environmental conditions, e.g., light stress, to prevent photochemical damage to the reaction center. We identified the LHC II degrading protease in...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2005-09, Vol.102 (38), p.13699-13704
Main Authors: Zelisko, A, Garcia-Lorenzo, M, Jackowski, G, Jansson, S, Funk, C
Format: Article
Language:English
Subjects:
acclimation
Acclimatization
Acclimatization - genetics
Aging - genetics
Apoproteins
Arabidopsis - enzymology
Arabidopsis - genetics
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Arabidopsis thaliana
Barley
Biochemistry
Biological Sciences
Chloroplasts
Flowers & plants
Gene expression regulation
Genome
Hordeum - enzymology
Hordeum - genetics
Hordeum vulgare
Leaves
Light
light harvesting complex
light intensity
Light-Harvesting Protein Complexes - metabolism
Metalloproteases - genetics
Metalloproteases - metabolism
Photosynthesis
photosystem II
Photosystem II Protein Complex - metabolism
Plant cells
Plants
Plants, Genetically Modified
Populus - enzymology
Populus - genetics
Populus trichocarpa
Proteases
protein degradation
proteinases
Proteins
proteolysis
senescence
Thylakoids
Zinc - metabolism
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Summary:Degradation of the most abundant membrane protein on earth, the light-harvesting complex of Photosystem II (LHC II), is highly regulated under various environmental conditions, e.g., light stress, to prevent photochemical damage to the reaction center. We identified the LHC II degrading protease in Arabidopsis thaliana as a Zn(2+)-dependent metalloprotease, activated by the removal of unknown extrinsic factors, similar to the proteolytic activity directed against Lhcb3 in barley. By using a reversed genetic approach, the chloroplast-targeted protease FtsH6 was identified as being responsible for the degradation. T-DNA KO A. thaliana mutants, lacking ftsH6, were unable to degrade either Lhcb3 during dark-induced senescence or Lhcb1 and Lhcb3 during highlight acclimation. The A. thaliana ftsH6 gene has a clear orthologue in the genome of Populus trichocarpa. It is likely that FtsH6 is a general LHC II protease and that FtsH6-dependent LHC II proteolysis is a feature of all higher plants.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0503472102