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The photosynthesis apparatus of European mistletoe (Viscum album)
European mistletoe (Viscum album) is known for its special mode of cellular respiration. It lacks the mitochondrial NADH dehydrogenase complex (Complex I of the respiratory chain) and has restricted capacities to generate mitochondrial adenosine triphosphate (ATP). Here, we present an investigation...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9614478/ https://www.ncbi.nlm.nih.gov/pubmed/35976139 http://dx.doi.org/10.1093/plphys/kiac377 |
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author | Schröder, Lucie Hegermann, Jan Pille, Patrick Braun, Hans-Peter |
author_facet | Schröder, Lucie Hegermann, Jan Pille, Patrick Braun, Hans-Peter |
author_sort | Schröder, Lucie |
collection | PubMed |
description | European mistletoe (Viscum album) is known for its special mode of cellular respiration. It lacks the mitochondrial NADH dehydrogenase complex (Complex I of the respiratory chain) and has restricted capacities to generate mitochondrial adenosine triphosphate (ATP). Here, we present an investigation of the V. album energy metabolism taking place in chloroplasts. Thylakoids were purified from young V. album leaves, and membrane-bound protein complexes were characterized by Blue native polyacrylamide gel electrophoresis as well as by the complexome profiling approach. Proteins were systematically identified by label-free quantitative shotgun proteomics. We identified >1,800 distinct proteins (accessible at https://complexomemap.de/va_leaves), including nearly 100 proteins forming part of the protein complexes involved in the light-dependent part of photosynthesis. The photosynthesis apparatus of V. album has distinct features: (1) comparatively low amounts of Photosystem I; (2) absence of the NDH complex (the chloroplast pendant of mitochondrial Complex I involved in cyclic electron transport (CET) around Photosystem I); (3) reduced levels of the proton gradient regulation 5 (PGR5) and proton gradient regulation 5-like 1 (PGRL1) proteins, which offer an alternative route for CET around Photosystem I; (4) comparable amounts of Photosystem II and the chloroplast ATP synthase complex to other seed plants. Our data suggest a restricted capacity for chloroplast ATP biosynthesis by the photophosphorylation process. This is in addition to the limited ATP supply by the mitochondria. We propose a view on mistletoe’s mode of life, according to which its metabolism relies to a greater extent on energy-rich compounds provided by the host trees. |
format | Online Article Text |
id | pubmed-9614478 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-96144782022-11-01 The photosynthesis apparatus of European mistletoe (Viscum album) Schröder, Lucie Hegermann, Jan Pille, Patrick Braun, Hans-Peter Plant Physiol Research Articles European mistletoe (Viscum album) is known for its special mode of cellular respiration. It lacks the mitochondrial NADH dehydrogenase complex (Complex I of the respiratory chain) and has restricted capacities to generate mitochondrial adenosine triphosphate (ATP). Here, we present an investigation of the V. album energy metabolism taking place in chloroplasts. Thylakoids were purified from young V. album leaves, and membrane-bound protein complexes were characterized by Blue native polyacrylamide gel electrophoresis as well as by the complexome profiling approach. Proteins were systematically identified by label-free quantitative shotgun proteomics. We identified >1,800 distinct proteins (accessible at https://complexomemap.de/va_leaves), including nearly 100 proteins forming part of the protein complexes involved in the light-dependent part of photosynthesis. The photosynthesis apparatus of V. album has distinct features: (1) comparatively low amounts of Photosystem I; (2) absence of the NDH complex (the chloroplast pendant of mitochondrial Complex I involved in cyclic electron transport (CET) around Photosystem I); (3) reduced levels of the proton gradient regulation 5 (PGR5) and proton gradient regulation 5-like 1 (PGRL1) proteins, which offer an alternative route for CET around Photosystem I; (4) comparable amounts of Photosystem II and the chloroplast ATP synthase complex to other seed plants. Our data suggest a restricted capacity for chloroplast ATP biosynthesis by the photophosphorylation process. This is in addition to the limited ATP supply by the mitochondria. We propose a view on mistletoe’s mode of life, according to which its metabolism relies to a greater extent on energy-rich compounds provided by the host trees. Oxford University Press 2022-08-17 /pmc/articles/PMC9614478/ /pubmed/35976139 http://dx.doi.org/10.1093/plphys/kiac377 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Schröder, Lucie Hegermann, Jan Pille, Patrick Braun, Hans-Peter The photosynthesis apparatus of European mistletoe (Viscum album) |
title | The photosynthesis apparatus of European mistletoe (Viscum album) |
title_full | The photosynthesis apparatus of European mistletoe (Viscum album) |
title_fullStr | The photosynthesis apparatus of European mistletoe (Viscum album) |
title_full_unstemmed | The photosynthesis apparatus of European mistletoe (Viscum album) |
title_short | The photosynthesis apparatus of European mistletoe (Viscum album) |
title_sort | photosynthesis apparatus of european mistletoe (viscum album) |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9614478/ https://www.ncbi.nlm.nih.gov/pubmed/35976139 http://dx.doi.org/10.1093/plphys/kiac377 |
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