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The structural basis for light acclimation in phycobilisome light harvesting systems in Porphyridium purpureum | The Keren Lab

The structural basis for light acclimation in phycobilisome light harvesting systems in Porphyridium purpureum

Citation:

Emma Joy Dodson, Ma, Jianfei , Szlejf, Maayan Suissa, Maroudas-Sklare, Naama , Paltiel, Yossi , Adir, Noam , Sun, Shan , Sui, Sen-Fang , and Keren, Nir . 2023. “The Structural Basis For Light Acclimation In Phycobilisome Light Harvesting Systems In Porphyridium Purpureum”, 6, 1, Pp. 1210. https://doi.org/10.1038/s42003-023-05586-4.

Abstract:

Photosynthetic organisms adapt to changing light conditions by manipulating their light harvesting complexes. Biophysical, biochemical, physiological and genetic aspects of these processes are studied extensively. The structural basis for these studies is lacking. In this study we address this gap in knowledge by focusing on phycobilisomes (PBS), which are large structures found in cyanobacteria and red algae. In this study we focus on the phycobilisomes (PBS), which are large structures found in cyanobacteria and red algae. Specifically, we examine red algae (Porphyridium purpureum) grown under a low light intensity (LL) and a medium light intensity (ML). Using cryo-electron microscopy, we resolve the structure of ML-PBS and compare it to the LL-PBS structure. The ML-PBS is 13.6 MDa, while the LL-PBS is larger (14.7 MDa). The LL-PBS structure have a higher number of closely coupled chromophore pairs, potentially the source of the red shifted fluorescence emission from LL-PBS. Interestingly, these differences do not significantly affect fluorescence kinetics parameters. This indicates that PBS systems can maintain similar fluorescence quantum yields despite an increase in LL-PBS chromophore numbers. These findings provide a structural basis to the processes by which photosynthetic organisms adapt to changing light conditions.
Last updated on 12/03/2023