Non-canonical localization of RubisCO under high-light conditions in the toxic cyanobacterium Microcystis aeruginosa PCC7806
- The frequent production of the hepatotoxin microcystin (MC) and its impact on the lifestyle of bloom-forming cyanobacteria are poorly understood. Here, we report that MC interferes with the assembly and the subcellular localization of RubisCO, in Microcystis aeruginosa PCC7806. Immunofluorescence, electron microscopic and cellular fractionation studies revealed a pronounced heterogeneity in the subcellular localization of RubisCO. At high cell density, RubisCO particles are largely separate from carboxysomes in M. aeruginosa and relocate to the cytoplasmic membrane under high-light conditions. We hypothesize that the binding of MC to RubisCO promotes its membrane association and enables an extreme versatility of the enzyme. Steady-state levels of the RubisCO CO2 fixation product 3-phosphoglycerate are significantly higher in the MC-producing wild type. We also detected noticeable amounts of the RubisCO oxygenase reaction product secreted into the medium that may support the mutual interaction of M. aeruginosa with its heterotrophicThe frequent production of the hepatotoxin microcystin (MC) and its impact on the lifestyle of bloom-forming cyanobacteria are poorly understood. Here, we report that MC interferes with the assembly and the subcellular localization of RubisCO, in Microcystis aeruginosa PCC7806. Immunofluorescence, electron microscopic and cellular fractionation studies revealed a pronounced heterogeneity in the subcellular localization of RubisCO. At high cell density, RubisCO particles are largely separate from carboxysomes in M. aeruginosa and relocate to the cytoplasmic membrane under high-light conditions. We hypothesize that the binding of MC to RubisCO promotes its membrane association and enables an extreme versatility of the enzyme. Steady-state levels of the RubisCO CO2 fixation product 3-phosphoglycerate are significantly higher in the MC-producing wild type. We also detected noticeable amounts of the RubisCO oxygenase reaction product secreted into the medium that may support the mutual interaction of M. aeruginosa with its heterotrophic microbial community.…
Verfasserangaben: | Tino Barchewitz, Arthur GuljamowGND, Sven MeißnerGND, Stefan TimmORCiDGND, Manja Henneberg, Otto BaumannORCiDGND, Martin HagemannORCiDGND, Elke DittmannORCiDGND |
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DOI: | https://doi.org/10.1111/1462-2920.14837 |
ISSN: | 1462-2912 |
ISSN: | 1462-2920 |
Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/31637830 |
Titel des übergeordneten Werks (Englisch): | Environmental microbiology |
Verlag: | Wiley |
Verlagsort: | Hoboken |
Publikationstyp: | Wissenschaftlicher Artikel |
Sprache: | Englisch |
Datum der Erstveröffentlichung: | 22.10.2019 |
Erscheinungsjahr: | 2019 |
Datum der Freischaltung: | 06.10.2020 |
Band: | 21 |
Ausgabe: | 12 |
Seitenanzahl: | 16 |
Erste Seite: | 4836 |
Letzte Seite: | 4851 |
Fördernde Institution: | Deutsche Forschungsgemeinschaft (DFG)German Research Foundation (DFG) [Di910/10-1, Ha2002/20-1]; DFGGerman Research Foundation (DFG) [SFB 1127]; HBFG program [GZ: INST 264/125-1 FUGG] |
Organisationseinheiten: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
DDC-Klassifikation: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Peer Review: | Referiert |
Publikationsweg: | Open Access |
Open Access / Hybrid Open-Access |