Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions
Autor(en): | Kramer, Manuela Rodriguez-Heredia, Melvin Saccon, Francesco Mosebach, Laura Twachtmann, Manuel Krieger-Liszkay, Anja Duffy, Chris Knell, Robert J. Finazzi, Giovanni Hanke, Guy Thomas |
Stichwörter: | Biology; C-TERMINAL TYROSINE; CHLAMYDOMONAS-REINHARDTII; CYCLIC PHOTOPHOSPHORYLATION; FERREDOXIN-NADP(+) OXIDOREDUCTASE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; Life Sciences & Biomedicine - Other Topics; NADP+ OXIDOREDUCTASE; PHOTOSYSTEM-I; PLASTOQUINONE REDUCTASE; PLUS OXIDOREDUCTASE; THYLAKOID MEMBRANES | Erscheinungsdatum: | 2021 | Herausgeber: | eLIFE SCIENCES PUBL LTD | Journal: | ELIFE | Volumen: | 10 | Zusammenfassung: | During photosynthesis, electron transport is necessary for carbon assimilation and must be regulated to minimize free radical damage. There is a longstanding controversy over the role of a critical enzyme in this process (ferredoxin:NADP(H) oxidoreductase, or FNR), and in particular its location within chloroplasts. Here we use immunogold labelling to prove that FNR previously assigned as soluble is in fact membrane associated. We combined this technique with a genetic approach in the model plant Arabidopsis to show that the distribution of this enzyme between different membrane regions depends on its interaction with specific tether proteins. We further demonstrate a correlation between the interaction of FNR with different proteins and the activity of alternative photosynthetic electron transport pathways. This supports a role for FNR location in regulating photosynthetic electron flow during the transition from dark to light. |
ISSN: | 2050084X | DOI: | 10.7554/eLife.56088 |
Zur Langanzeige
Seitenaufrufe
6
Letzte Woche
0
0
Letzter Monat
1
1
geprüft am 10.05.2024