PSI of the colonial alga Botryococcus braunii has an unusually large antenna size

Tomas E. van den Berg; Rameez Arshad; Wojciech J. Nawrocki; Egbert J. Boekema; Roman Kouril; Roberta Croce

doi:10.1104/pp.20.00823

PSI of the colonial alga Botryococcus braunii has an unusually large antenna size

Tomas E. van den Berg, Rameez Arshad, Wojciech J. Nawrocki, Egbert J. Boekema, Roman Kouril, Roberta Croce^*

^*Corresponding author for this work

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

PSI is an essential component of the photosynthetic apparatus of oxygenic photosynthesis. While most of its subunits are conserved, recent data have shown that the arrangement of the light-harvesting complexes I (LHCIs) differs substantially in different organisms. Here we studied the PSI-LHCI supercomplex of Botryococccus braunii, a colonial green alga with potential for lipid and sugar production, using functional analysis and single-particle electron microscopy of the isolated PSI-LHCI supercomplexes complemented by time-resolved fluorescence spectroscopy in vivo. We established that the largest purified PSI-LHCI supercomplex contains 10 LHCIs (;240 chlorophylls). However, electron microscopy showed heterogeneity in the particles and a total of 13 unique binding sites for the LHCIs around the PSI core. Time-resolved fluorescence spectroscopy indicated that the PSI antenna size in vivo is even larger than that of the purified complex. Based on the comparison of the known PSI structures, we propose that PSI in B. braunii can bind LHCIs at all known positions surrounding the core. This organization maximizes the antenna size while maintaining fast excitation energy transfer, and thus high trapping efficiency, within the complex.

Original language	English
Pages (from-to)	2040-2051
Number of pages	12
Journal	Plant physiology
Volume	184
Issue number	4
DOIs	https://doi.org/10.1104/pp.20.00823
Publication status	Published - Dec 2020

Funding

1This work was supported by the Netherlands Organization of Scientific Research (Vici grant to R.C.), the BioSolar Cell Program (grant to R.C., cofinanced by the Dutch Ministry of Economic Affairs), the European Commission Marie Curie Actions Individual Fellowship (grant no. 799083 to W.J.N.), the European Union’s Horizon 2020 Research and Innovation Program (grant no. 675006 to R.C., R.A., R.K., E.J.B.), and the European Regional Development Fund project “Plants as a tool for sustainable global development” (project no.CZ. 02.1.01/0.0/0.0/16_019/0000827). 2Senior author. 3Author for contact: [email protected].

Funders	Funder number
BioSolar Cell Program
European Commission Marie Curie Actions
Horizon 2020 Framework Programme	675006, 799083
Ministerie van Economische Zaken
Nederlandse Organisatie voor Wetenschappelijk Onderzoek
European Regional Development Fund	16_019/0000827

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title = "PSI of the colonial alga Botryococcus braunii has an unusually large antenna size",

abstract = "PSI is an essential component of the photosynthetic apparatus of oxygenic photosynthesis. While most of its subunits are conserved, recent data have shown that the arrangement of the light-harvesting complexes I (LHCIs) differs substantially in different organisms. Here we studied the PSI-LHCI supercomplex of Botryococccus braunii, a colonial green alga with potential for lipid and sugar production, using functional analysis and single-particle electron microscopy of the isolated PSI-LHCI supercomplexes complemented by time-resolved fluorescence spectroscopy in vivo. We established that the largest purified PSI-LHCI supercomplex contains 10 LHCIs (;240 chlorophylls). However, electron microscopy showed heterogeneity in the particles and a total of 13 unique binding sites for the LHCIs around the PSI core. Time-resolved fluorescence spectroscopy indicated that the PSI antenna size in vivo is even larger than that of the purified complex. Based on the comparison of the known PSI structures, we propose that PSI in B. braunii can bind LHCIs at all known positions surrounding the core. This organization maximizes the antenna size while maintaining fast excitation energy transfer, and thus high trapping efficiency, within the complex.",

author = "{van den Berg}, {Tomas E.} and Rameez Arshad and Nawrocki, {Wojciech J.} and Boekema, {Egbert J.} and Roman Kouril and Roberta Croce",

year = "2020",

month = dec,

doi = "10.1104/pp.20.00823",

language = "English",

volume = "184",

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T1 - PSI of the colonial alga Botryococcus braunii has an unusually large antenna size

AU - van den Berg, Tomas E.

AU - Arshad, Rameez

AU - Nawrocki, Wojciech J.

AU - Boekema, Egbert J.

AU - Kouril, Roman

AU - Croce, Roberta

PY - 2020/12

Y1 - 2020/12

N2 - PSI is an essential component of the photosynthetic apparatus of oxygenic photosynthesis. While most of its subunits are conserved, recent data have shown that the arrangement of the light-harvesting complexes I (LHCIs) differs substantially in different organisms. Here we studied the PSI-LHCI supercomplex of Botryococccus braunii, a colonial green alga with potential for lipid and sugar production, using functional analysis and single-particle electron microscopy of the isolated PSI-LHCI supercomplexes complemented by time-resolved fluorescence spectroscopy in vivo. We established that the largest purified PSI-LHCI supercomplex contains 10 LHCIs (;240 chlorophylls). However, electron microscopy showed heterogeneity in the particles and a total of 13 unique binding sites for the LHCIs around the PSI core. Time-resolved fluorescence spectroscopy indicated that the PSI antenna size in vivo is even larger than that of the purified complex. Based on the comparison of the known PSI structures, we propose that PSI in B. braunii can bind LHCIs at all known positions surrounding the core. This organization maximizes the antenna size while maintaining fast excitation energy transfer, and thus high trapping efficiency, within the complex.

AB - PSI is an essential component of the photosynthetic apparatus of oxygenic photosynthesis. While most of its subunits are conserved, recent data have shown that the arrangement of the light-harvesting complexes I (LHCIs) differs substantially in different organisms. Here we studied the PSI-LHCI supercomplex of Botryococccus braunii, a colonial green alga with potential for lipid and sugar production, using functional analysis and single-particle electron microscopy of the isolated PSI-LHCI supercomplexes complemented by time-resolved fluorescence spectroscopy in vivo. We established that the largest purified PSI-LHCI supercomplex contains 10 LHCIs (;240 chlorophylls). However, electron microscopy showed heterogeneity in the particles and a total of 13 unique binding sites for the LHCIs around the PSI core. Time-resolved fluorescence spectroscopy indicated that the PSI antenna size in vivo is even larger than that of the purified complex. Based on the comparison of the known PSI structures, we propose that PSI in B. braunii can bind LHCIs at all known positions surrounding the core. This organization maximizes the antenna size while maintaining fast excitation energy transfer, and thus high trapping efficiency, within the complex.

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PSI of the colonial alga Botryococcus braunii has an unusually large antenna size

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