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| Main Authors: | , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Nature communications
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41422266/ |
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| _version_ | 1868266108341977088 |
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| author | Si, Long Zhang, Yingyue Su, Xiaodong Zhao, Xuelin An, Xiaomin Liu, Lu-Ning Cao, Peng Li, Mei |
| author_facet | Si, Long Zhang, Yingyue Su, Xiaodong Zhao, Xuelin An, Xiaomin Liu, Lu-Ning Cao, Peng Li, Mei Si, Long Zhang, Yingyue Su, Xiaodong Zhao, Xuelin An, Xiaomin Liu, Lu-Ning Cao, Peng Li, Mei |
| collection | PubMed - marine biology |
| contents | Structural basis for the assembly and energy transfer between the cyanobacterial PSI core and the double-layered IsiA proteins. Si, Long Zhang, Yingyue Su, Xiaodong Zhao, Xuelin An, Xiaomin Liu, Lu-Ning Cao, Peng Li, Mei Photosystem I Protein Complex Bacterial Proteins Energy Transfer Microscopy, Atomic Force Iron Thermosynechococcus Cyanobacteria Light-Harvesting Protein Complexes Models, Molecular Synechococcus Iron-limitation is a common stress factor in natural environments. To survive under iron-starved conditions, cyanobacteria overexpress iron stress-induced protein A (IsiA), which is crucial for light-harvesting and photoprotection. Multiple IsiA proteins form a single- or double-layered architecture encircling the photosystem I (PSI) core, forming various PSI-IsiA supercomplexes. The assembly and energy transfer mechanisms of double-layered PSI-IsiA supercomplexes remain unelucidated. Here, we present high-resolution structures of two PSI-IsiA supercomplexes isolated from the cyanobacterium Thermosynechococcus elongatus BP-1 cultured under iron-starved conditions. The PSI-IsiA complex contains a trimeric PSI core surrounded by 43 IsiA subunits assembled into a closed double-ring. The PSI-IsiA complex contains 13 IsiA proteins arranged in a double-layered architecture attached to the monomeric PSI core. Atomic force microscopy demonstrates the presence and distribution of different PSI-IsiA complexes within native thylakoid membranes isolated from iron-starved cells. Our findings provide insights into the structural variability and adaptive mechanisms of PSI-IsiA complexes. |
| format | Artículo científico |
| id | pubmed_41422266 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Nature communications |
| record_format | pubmed |
| spellingShingle | Structural basis for the assembly and energy transfer between the cyanobacterial PSI core and the double-layered IsiA proteins. Si, Long Zhang, Yingyue Su, Xiaodong Zhao, Xuelin An, Xiaomin Liu, Lu-Ning Cao, Peng Li, Mei Photosystem I Protein Complex Bacterial Proteins Energy Transfer Microscopy, Atomic Force Iron Thermosynechococcus Cyanobacteria Light-Harvesting Protein Complexes Models, Molecular Synechococcus Structural basis for the assembly and energy transfer between the cyanobacterial PSI core and the double-layered IsiA proteins. Si, Long Zhang, Yingyue Su, Xiaodong Zhao, Xuelin An, Xiaomin Liu, Lu-Ning Cao, Peng Li, Mei Photosystem I Protein Complex Bacterial Proteins Energy Transfer Microscopy, Atomic Force Iron Thermosynechococcus Cyanobacteria Light-Harvesting Protein Complexes Models, Molecular Synechococcus Iron-limitation is a common stress factor in natural environments. To survive under iron-starved conditions, cyanobacteria overexpress iron stress-induced protein A (IsiA), which is crucial for light-harvesting and photoprotection. Multiple IsiA proteins form a single- or double-layered architecture encircling the photosystem I (PSI) core, forming various PSI-IsiA supercomplexes. The assembly and energy transfer mechanisms of double-layered PSI-IsiA supercomplexes remain unelucidated. Here, we present high-resolution structures of two PSI-IsiA supercomplexes isolated from the cyanobacterium Thermosynechococcus elongatus BP-1 cultured under iron-starved conditions. The PSI-IsiA complex contains a trimeric PSI core surrounded by 43 IsiA subunits assembled into a closed double-ring. The PSI-IsiA complex contains 13 IsiA proteins arranged in a double-layered architecture attached to the monomeric PSI core. Atomic force microscopy demonstrates the presence and distribution of different PSI-IsiA complexes within native thylakoid membranes isolated from iron-starved cells. Our findings provide insights into the structural variability and adaptive mechanisms of PSI-IsiA complexes. |
| title | Structural basis for the assembly and energy transfer between the cyanobacterial PSI core and the double-layered IsiA proteins. |
| topic | Photosystem I Protein Complex Bacterial Proteins Energy Transfer Microscopy, Atomic Force Iron Thermosynechococcus Cyanobacteria Light-Harvesting Protein Complexes Models, Molecular Synechococcus |
| url | https://pubmed.ncbi.nlm.nih.gov/41422266/ |