Conspicuous chloroplast with light harvesting-photosystem I/II megacomplex in marine Prorocentrum cordatum

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

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  • Constructor University Bremen
  • Carl von Ossietzky Universität Oldenburg
  • Ludwig-Maximilians-Universität München (LMU)
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Details

OriginalspracheEnglisch
Seiten (von - bis)306-325
Seitenumfang20
FachzeitschriftPlant physiology
Jahrgang195
Ausgabenummer1
Frühes Online-Datum8 Feb. 2024
PublikationsstatusVeröffentlicht - Mai 2024

Abstract

Marine photosynthetic (micro)organisms drive multiple biogeochemical cycles and display a large diversity. Among them, the bloom-forming, free-living dinoflagellate Prorocentrum cordatum CCMP 1329 (formerly P. minimum) stands out with its distinct cell biological features. Here, we obtained insights into the structural properties of the chloroplast and the photosynthetic machinery of P. cordatum using microscopic and proteogenomic approaches. High-resolution FIB/SEM analysis revealed a single large chloroplast (∼40% of total cell volume) with a continuous barrel-like structure, completely lining the inner face of the cell envelope and enclosing a single reticular mitochondrium, the Golgi apparatus, as well as diverse storage inclusions. Enriched thylakoid membrane fractions of P. cordatum were comparatively analyzed with those of the well-studied model-species Arabidopsis (Arabidopsis thaliana) using 2D BN DIGE. Strikingly, P. cordatum possessed a large photosystem-light harvesting megacomplex (>1.5 MDa), which is dominated by photosystems I and II (PSI, PSII), chloroplast complex (CCI), and chlorophylla-b (chla-b) binding light harvesting complex proteins (LhcPs). This finding parallels the absence of grana in its chloroplast and distinguishes from the predominant separation of PSI and PSII complexes in A. thaliana, indicating a different mode of flux balancing. Except for the core elements of the ATP synthase and the cytb6f-complex, the composition of the other complexes (PSI, PSII, and pigment-binding proteins (PBPs)) of P. cordatum differed markedly from those of A. thaliana. Furthermore, a high number of PBPs was detected, accounting for a large share of the total proteomic data (∼65%) and potentially providing P. cordatum with flexible adaptation to changing light regimes.

ASJC Scopus Sachgebiete

  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Genetik
  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Physiologie
  • Agrar- und Biowissenschaften (insg.)
  • Pflanzenkunde

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Conspicuous chloroplast with light harvesting-photosystem I/II megacomplex in marine Prorocentrum cordatum. / Kalvelage, Jana; Wöhlbrand, Lars; Senkler, Jennifer et al.
in: Plant physiology, Jahrgang 195, Nr. 1, 05.2024, S. 306-325.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Kalvelage, J, Wöhlbrand, L, Senkler, J, Schumacher, J, Ditz, N, Bischof, K, Winklhofer, M, Klingl, A, Braun, H-P & Rabus, R 2024, 'Conspicuous chloroplast with light harvesting-photosystem I/II megacomplex in marine Prorocentrum cordatum', Plant physiology, Jg. 195, Nr. 1, S. 306-325. https://doi.org/10.1093/plphys/kiae052
Kalvelage, J., Wöhlbrand, L., Senkler, J., Schumacher, J., Ditz, N., Bischof, K., Winklhofer, M., Klingl, A., Braun, H.-P., & Rabus, R. (2024). Conspicuous chloroplast with light harvesting-photosystem I/II megacomplex in marine Prorocentrum cordatum. Plant physiology, 195(1), 306-325. https://doi.org/10.1093/plphys/kiae052
Kalvelage J, Wöhlbrand L, Senkler J, Schumacher J, Ditz N, Bischof K et al. Conspicuous chloroplast with light harvesting-photosystem I/II megacomplex in marine Prorocentrum cordatum. Plant physiology. 2024 Mai;195(1):306-325. Epub 2024 Feb 8. doi: 10.1093/plphys/kiae052
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title = "Conspicuous chloroplast with light harvesting-photosystem I/II megacomplex in marine Prorocentrum cordatum",
abstract = "Marine photosynthetic (micro)organisms drive multiple biogeochemical cycles and display a large diversity. Among them, the bloom-forming, free-living dinoflagellate Prorocentrum cordatum CCMP 1329 (formerly P. minimum) stands out with its distinct cell biological features. Here, we obtained insights into the structural properties of the chloroplast and the photosynthetic machinery of P. cordatum using microscopic and proteogenomic approaches. High-resolution FIB/SEM analysis revealed a single large chloroplast (∼40% of total cell volume) with a continuous barrel-like structure, completely lining the inner face of the cell envelope and enclosing a single reticular mitochondrium, the Golgi apparatus, as well as diverse storage inclusions. Enriched thylakoid membrane fractions of P. cordatum were comparatively analyzed with those of the well-studied model-species Arabidopsis (Arabidopsis thaliana) using 2D BN DIGE. Strikingly, P. cordatum possessed a large photosystem-light harvesting megacomplex (>1.5 MDa), which is dominated by photosystems I and II (PSI, PSII), chloroplast complex (CCI), and chlorophylla-b (chla-b) binding light harvesting complex proteins (LhcPs). This finding parallels the absence of grana in its chloroplast and distinguishes from the predominant separation of PSI and PSII complexes in A. thaliana, indicating a different mode of flux balancing. Except for the core elements of the ATP synthase and the cytb6f-complex, the composition of the other complexes (PSI, PSII, and pigment-binding proteins (PBPs)) of P. cordatum differed markedly from those of A. thaliana. Furthermore, a high number of PBPs was detected, accounting for a large share of the total proteomic data (∼65%) and potentially providing P. cordatum with flexible adaptation to changing light regimes.",
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T1 - Conspicuous chloroplast with light harvesting-photosystem I/II megacomplex in marine Prorocentrum cordatum

AU - Kalvelage, Jana

AU - Wöhlbrand, Lars

AU - Senkler, Jennifer

AU - Schumacher, Julian

AU - Ditz, Noah

AU - Bischof, Kai

AU - Winklhofer, Michael

AU - Klingl, Andreas

AU - Braun, Hans-Peter

AU - Rabus, Ralf

N1 - © The Author(s) 2024. Published by Oxford University Press on behalf of American Society of Plant Biologists.

PY - 2024/5

Y1 - 2024/5

N2 - Marine photosynthetic (micro)organisms drive multiple biogeochemical cycles and display a large diversity. Among them, the bloom-forming, free-living dinoflagellate Prorocentrum cordatum CCMP 1329 (formerly P. minimum) stands out with its distinct cell biological features. Here, we obtained insights into the structural properties of the chloroplast and the photosynthetic machinery of P. cordatum using microscopic and proteogenomic approaches. High-resolution FIB/SEM analysis revealed a single large chloroplast (∼40% of total cell volume) with a continuous barrel-like structure, completely lining the inner face of the cell envelope and enclosing a single reticular mitochondrium, the Golgi apparatus, as well as diverse storage inclusions. Enriched thylakoid membrane fractions of P. cordatum were comparatively analyzed with those of the well-studied model-species Arabidopsis (Arabidopsis thaliana) using 2D BN DIGE. Strikingly, P. cordatum possessed a large photosystem-light harvesting megacomplex (>1.5 MDa), which is dominated by photosystems I and II (PSI, PSII), chloroplast complex (CCI), and chlorophylla-b (chla-b) binding light harvesting complex proteins (LhcPs). This finding parallels the absence of grana in its chloroplast and distinguishes from the predominant separation of PSI and PSII complexes in A. thaliana, indicating a different mode of flux balancing. Except for the core elements of the ATP synthase and the cytb6f-complex, the composition of the other complexes (PSI, PSII, and pigment-binding proteins (PBPs)) of P. cordatum differed markedly from those of A. thaliana. Furthermore, a high number of PBPs was detected, accounting for a large share of the total proteomic data (∼65%) and potentially providing P. cordatum with flexible adaptation to changing light regimes.

AB - Marine photosynthetic (micro)organisms drive multiple biogeochemical cycles and display a large diversity. Among them, the bloom-forming, free-living dinoflagellate Prorocentrum cordatum CCMP 1329 (formerly P. minimum) stands out with its distinct cell biological features. Here, we obtained insights into the structural properties of the chloroplast and the photosynthetic machinery of P. cordatum using microscopic and proteogenomic approaches. High-resolution FIB/SEM analysis revealed a single large chloroplast (∼40% of total cell volume) with a continuous barrel-like structure, completely lining the inner face of the cell envelope and enclosing a single reticular mitochondrium, the Golgi apparatus, as well as diverse storage inclusions. Enriched thylakoid membrane fractions of P. cordatum were comparatively analyzed with those of the well-studied model-species Arabidopsis (Arabidopsis thaliana) using 2D BN DIGE. Strikingly, P. cordatum possessed a large photosystem-light harvesting megacomplex (>1.5 MDa), which is dominated by photosystems I and II (PSI, PSII), chloroplast complex (CCI), and chlorophylla-b (chla-b) binding light harvesting complex proteins (LhcPs). This finding parallels the absence of grana in its chloroplast and distinguishes from the predominant separation of PSI and PSII complexes in A. thaliana, indicating a different mode of flux balancing. Except for the core elements of the ATP synthase and the cytb6f-complex, the composition of the other complexes (PSI, PSII, and pigment-binding proteins (PBPs)) of P. cordatum differed markedly from those of A. thaliana. Furthermore, a high number of PBPs was detected, accounting for a large share of the total proteomic data (∼65%) and potentially providing P. cordatum with flexible adaptation to changing light regimes.

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U2 - 10.1093/plphys/kiae052

DO - 10.1093/plphys/kiae052

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JF - Plant physiology

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