The photosynthesis apparatus of European mistletoe (Viscum album).


Journal

Plant physiology
ISSN: 1532-2548
Titre abrégé: Plant Physiol
Pays: United States
ID NLM: 0401224

Informations de publication

Date de publication:
27 10 2022
Historique:
received: 07 06 2022
accepted: 19 07 2022
pubmed: 18 8 2022
medline: 1 11 2022
entrez: 17 8 2022
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 35976139
pii: 6670632
doi: 10.1093/plphys/kiac377
pmc: PMC9614478
doi:

Substances chimiques

Photosystem I Protein Complex 0
Arabidopsis Proteins 0
Protons 0
Electron Transport Complex I EC 7.1.1.2
Adenosine Triphosphate 8L70Q75FXE

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1896-1914

Informations de copyright

© The Author(s) 2022. Published by Oxford University Press on behalf of American Society of Plant Biologists.

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Auteurs

Lucie Schröder (L)

Institut für Pflanzgenetik, Leibniz Universität Hannover, Herrenhäuser Str. 2, 30419 Hannover, Germany.

Jan Hegermann (J)

Institut für Funktionelle und Angewandte Anatomie, Medizinische Hochschule Hannover, Carl-Neuberg-Straße 1, 30625 Hannover, Germany.

Patrick Pille (P)

Institut für Pflanzgenetik, Leibniz Universität Hannover, Herrenhäuser Str. 2, 30419 Hannover, Germany.

Hans-Peter Braun (HP)

Institut für Pflanzgenetik, Leibniz Universität Hannover, Herrenhäuser Str. 2, 30419 Hannover, Germany.

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Classifications MeSH