ArticlePhotosynthesis research2016
β-Carotene influences the phycobilisome antenna of cyanobacterium Synechocystis sp. PCC 6803.
Article in Photosynthesis research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Changes in light-harvesting and energy-transfer processes of the chlorophyll d-dominated cyanobacterium Acaryochloris marina in response to different light qualities.Photosynthesis research · 2025Article
- Reconstruction of the absorption spectrum of Synechocystis sp. PCC 6803 optical mutants from the in vivo signature of individual pigments.Photosynthesis research · 2021Article
- Phycobilisome integrity and functionality in lipid unsaturation and xanthophyll mutants in Synechocystis.Photosynthesis research · 2020Article
- Lipid and carotenoid cooperation-driven adaptation to light and temperature stress in Synechocystis sp. PCC6803.Biochimica et biophysica acta. Bioenergetics · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigated the relation between the carotenoid composition and the structure of phycobilisome (PBS) antenna of cyanobacterium Synechocystis sp. PCC 6803. PBS is a large soluble protein complex enhances the light harvesting efficiency of the cells. It is composed of a central allophycocyanin core and radial phycocyanin rods, but it does not contain carotenoids. However, the absence or low level of carotenoids were previously shown to lead the co-existence of unconnected rod units and assembled PBS with shorter peripheral rods. Here we show that the lack of β-carotene, but not of xanthophylls or the distortion of photosystem structure, evoked unconnected rods. Thus, these essential β-carotene molecules are not bound by Photosystem I or Photosystem II. Our results do not show correlation between the reactive oxygen species (ROS) and PBS distortion despite the higher singlet oxygen producing capacity and light sensitivity of the mutant cells. Reduced cellular level of those linker proteins attaching the rod units together was also observed, but the direct damage of the linkers by ROS are not supported by our data. Enzymatic PBS proteolysis induced by nitrogen starvation in carotenoid mutant cells revealed a retarded degradation of the unconnected rod units.
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