Pigment-protein complexes are organized into stable microdomains in cyanobacterial thylakoids
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
31344362
DOI
10.1016/j.bbabio.2019.07.008
PII: S0005-2728(19)30090-8
Knihovny.cz E-resources
- Keywords
- Confocal microscopy, Cyanobacteria, Membrane heterogeneity, Microdomains, Photosynthesis, Photosystems, Population heterogeneity, Thylakoid membrane,
- MeSH
- Bacterial Proteins metabolism MeSH
- Photosynthesis physiology MeSH
- Photosystem I Protein Complex metabolism MeSH
- Photosystem II Protein Complex metabolism MeSH
- Phycobilisomes metabolism MeSH
- Microscopy, Confocal MeSH
- Membrane Microdomains metabolism MeSH
- Synechocystis MeSH
- Thylakoids metabolism MeSH
- Imaging, Three-Dimensional MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Photosystem I Protein Complex MeSH
- Photosystem II Protein Complex MeSH
- Phycobilisomes MeSH
Thylakoids are the place of the light-photosynthetic reactions. To gain maximal efficiency, these reactions are conditional to proper pigment-pigment and protein-protein interactions. In higher plants thylakoids, the interactions lead to a lateral asymmetry in localization of protein complexes (i.e. granal/stromal thylakoids) that have been defined as a domain-like structures characteristic by different biochemical composition and function (Albertsson P-Å. 2001,Trends Plant Science 6: 349-354). We explored this complex organization of thylakoid pigment-proteins at single cell level in the cyanobacterium Synechocystis sp. PCC 6803. Our 3D confocal images captured heterogeneous distribution of all main photosynthetic pigment-protein complexes (PPCs), Photosystem I (fluorescently tagged by YFP), Photosystem II and Phycobilisomes. The acquired images depicted cyanobacterial thylakoid membrane as a stable, mosaic-like structure formed by microdomains (MDs). These microcompartments are of sub-micrometer in sizes (~0.5-1.5 μm), typical by particular PPCs ratios and importantly without full segregation of observed complexes. The most prevailing MD is represented by MD with high Photosystem I content which allows also partial separation of Photosystems like in higher plants thylakoids. We assume that MDs stability (in minutes) provides optimal conditions for efficient excitation/electron transfer. The cyanobacterial MDs thus define thylakoid membrane organization as a system controlled by co-localization of three main PPCs leading to formation of thylakoid membrane mosaic. This organization might represent evolutional and functional precursor for the granal/stromal spatial heterogeneity in photosystems that is typical for higher plant thylakoids.
References provided by Crossref.org
Phycobilisome protein ApcG interacts with PSII and regulates energy transfer in Synechocystis
Fast Diffusion of the Unassembled PetC1-GFP Protein in the Cyanobacterial Thylakoid Membrane
Plasticity of Cyanobacterial Thylakoid Microdomains Under Variable Light Conditions