Structural basis for energy transfer in a huge diatom PSI-FCPI supercomplex

Xu, Caizhe; Pi, Xiong; Huang, Ya-Wen; Han, Guangye; Chen, Xiaobo; Qin, Xiaochun; Huang, Guoqiang; Zhao, Songhao; Yang, Yanyan; Kuang, Tingyun; Wang, Wenda; Sui, Sen-Fang; Shen, Jian Ren

doi:10.1038/s41467-020-18867-x

Cited by 72 publications

(152 citation statements)

References 54 publications

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“…Dissolved FCP crystals excite at 436, 465, and 540 nm and the fluorescence emission wavelength is 676 nm [16]. The fluorescence spectrum scan of PSI-FCPI showed that there is a single emission wavelength at about 708 nm, which is similar to our results [27]. The fluorescence emission spectra of PSII-FCPII excite at 425, 459, and 500 nm, measuring at 77 K. The main peak is located at 694 nm [28,29].…”

Section: P Tricornutum Has a Specific Emission Wavelengthsupporting

confidence: 88%

“…These results illustrate that the emission fluorescence of P. tricornutum cells at 710 nm should not be emitted by a single pigment and is most likely a special fluorescence emission peak of the photosynthetic system complex structure in diatoms. In recent reports, the structures of FCP complex, PSI-FCPI, and PSII-FCPII were analyzed by cryo-electron microscopy [16,[27][28][29]. In the separation and purification of these complex structures, fluorescence emission spectra at 77 K were measured using a fluorescence spectrophotometer.…”

Section: P Tricornutum Has a Specific Emission Wavelengthmentioning

confidence: 99%

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Rapid Sorting of Fucoxanthin-Producing Phaeodactylum tricornutum Mutants by Flow Cytometry

et al. 2021

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Fucoxanthin, which is widely found in seaweeds and diatoms, has many benefits to human health, such as anti-diabetes, anti-obesity, and anti-inflammatory physiological activities. However, the low content of fucoxanthin in brown algae and diatoms limits the commercialization of this product. In this study, we introduced an excitation light at 488 nm to analyze the emitted fluorescence of Phaeodactylum tricornutum, a diatom model organism rich in fucoxanthin. We observed a unique spectrum peak at 710 nm and found a linear correlation between fucoxanthin content and the mean fluorescence intensity. We subsequently used flow cytometry to screen high-fucoxanthin-content mutants created by heavy ion irradiation. After 20 days of cultivation, the fucoxanthin content of sorted cells was 25.5% higher than in the wild type. This method provides an efficient, rapid, and high-throughput approach to screen fucoxanthin-overproducing mutants.

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Section: P Tricornutum Has a Specific Emission Wavelengthsupporting

confidence: 88%

Section: P Tricornutum Has a Specific Emission Wavelengthmentioning

confidence: 99%

Rapid Sorting of Fucoxanthin-Producing Phaeodactylum tricornutum Mutants by Flow Cytometry

et al. 2021

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“…In contrast, PSI cores from eukaryotic algae and higher plants exist as a monomer, which is associated with various membrane-spanning light-harvesting complex I (LHCI), forming PSI–LHCI supercomplexes. The structures of PSI–LHCI supercomplexes have been solved from various eukaryotic organisms such as red algae 6 , diatoms 7 , 8 , green algae 9 – 11 , and land plants 12 – 14 . These studies showed that the PSI core is relatively conserved during more than 2.5 billion years of evolution, whereas there is a large diversity in the pigment and protein compositions of LHCI from different organisms 15 .…”

Section: Introductionmentioning

confidence: 99%

Antenna arrangement and energy-transfer pathways of PSI–LHCI from the moss Physcomitrella patens

et al. 2021

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Plants harvest light energy utilized for photosynthesis by light-harvesting complex I and II (LHCI and LHCII) surrounding photosystem I and II (PSI and PSII), respectively. During the evolution of green plants, moss is at an evolutionarily intermediate position from aquatic photosynthetic organisms to land plants, being the first photosynthetic organisms that landed. Here, we report the structure of the PSI–LHCI supercomplex from the moss Physcomitrella patens (Pp) at 3.23 Å resolution solved by cryo-electron microscopy. Our structure revealed that four Lhca subunits are associated with the PSI core in an order of Lhca1–Lhca5–Lhca2–Lhca3. This number is much decreased from 8 to 10, the number of subunits in most green algal PSI–LHCI, but the same as those of land plants. Although Pp PSI–LHCI has a similar structure as PSI–LHCI of land plants, it has Lhca5, instead of Lhca4, in the second position of Lhca, and several differences were found in the arrangement of chlorophylls among green algal, moss, and land plant PSI–LHCI. One chlorophyll, PsaF–Chl 305, which is found in the moss PSI–LHCI, is located at the gap region between the two middle Lhca subunits and the PSI core, and therefore may make the excitation energy transfer from LHCI to the core more efficient than that of land plants. On the other hand, energy-transfer paths at the two side Lhca subunits are relatively conserved. These results provide a structural basis for unravelling the mechanisms of light-energy harvesting and transfer in the moss PSI–LHCI, as well as important clues on the changes of PSI–LHCI after landing.

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“…The crystal structure of PSI‐LHCI supercomplex from higher plants was also analyzed at 2.6–2.8 Å resolutions (Mazor et al, 2015, 2017; Qin et al, 2015; Pan et al, 2018). Recently, the structure of PSI‐LHCI from a red alga (Antoshvili et al, 2018; Pi et al, 2018), a diatom (Nagao et al, 2020; Xu et al, 2020) and green algae (Qin et al, 2019; Su et al, 2019; Suga et al, 2019) have been solved by cryo‐EM. These studies revealed that the cofactor arrangement of the PSI core involved in electron transfer is highly conserved from cyanobacteria to higher plants, which occurs in two branches of the core beginning from P 700 to primary and secondary electron acceptors A Acc , A 0 , A 1 , and finally to the three Fe 4 S 4 clusters (Nelson and Junge, 2015).…”

Section: Introductionmentioning

confidence: 99%

Structure of plant photosystem I−light harvesting complex I supercomplex at 2.4 Å resolution

Wang

et al. 2021

JIPB

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Photosystem I (PSI) is one of the two photosystems in photosynthesis, and performs a series of electron transfer reactions leading to the reduction of ferredoxin. In higher plants, PSI is surrounded by four light‐harvesting complex I (LHCI) subunits, which harvest and transfer energy efficiently to the PSI core. The crystal structure of PSI‐LHCI supercomplex has been analyzed up to 2.6 Å resolution, providing much information on the arrangement of proteins and cofactors in this complicated supercomplex. Here we have optimized crystallization conditions, and analyzed the crystal structure of PSI‐LHCI at 2.4 Å resolution. Our structure showed some shift of the LHCI, especially the Lhca4 subunit, away from the PSI core, suggesting the indirect connection and inefficiency of energy transfer from this Lhca subunit to the PSI core. We identified five new lipids in the structure, most of them are located in the gap region between the Lhca subunits and the PSI core. These lipid molecules may play important roles in binding of the Lhca subunits to the core, as well as in the assembly of the supercomplex. The present results thus provide novel information for the elucidation of the mechanisms for the light‐energy harvesting, transfer and assembly of this supercomplex.

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Structural basis for energy transfer in a huge diatom PSI-FCPI supercomplex

Cited by 72 publications

References 54 publications

Rapid Sorting of Fucoxanthin-Producing Phaeodactylum tricornutum Mutants by Flow Cytometry

Rapid Sorting of Fucoxanthin-Producing Phaeodactylum tricornutum Mutants by Flow Cytometry

Antenna arrangement and energy-transfer pathways of PSI–LHCI from the moss Physcomitrella patens

Structure of plant photosystem I−light harvesting complex I supercomplex at 2.4 Å resolution

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