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Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions
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 wit...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7984839/ https://www.ncbi.nlm.nih.gov/pubmed/33685582 http://dx.doi.org/10.7554/eLife.56088 |
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author | Kramer, Manuela Rodriguez-Heredia, Melvin Saccon, Francesco Mosebach, Laura Twachtmann, Manuel Krieger-Liszkay, Anja Duffy, Chris Knell, Robert J Finazzi, Giovanni Hanke, Guy Thomas |
author_facet | Kramer, Manuela Rodriguez-Heredia, Melvin Saccon, Francesco Mosebach, Laura Twachtmann, Manuel Krieger-Liszkay, Anja Duffy, Chris Knell, Robert J Finazzi, Giovanni Hanke, Guy Thomas |
author_sort | Kramer, Manuela |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7984839 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-79848392021-03-24 Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions Kramer, Manuela Rodriguez-Heredia, Melvin Saccon, Francesco Mosebach, Laura Twachtmann, Manuel Krieger-Liszkay, Anja Duffy, Chris Knell, Robert J Finazzi, Giovanni Hanke, Guy Thomas eLife Plant Biology 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. eLife Sciences Publications, Ltd 2021-03-09 /pmc/articles/PMC7984839/ /pubmed/33685582 http://dx.doi.org/10.7554/eLife.56088 Text en © 2021, Kramer et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Plant Biology Kramer, Manuela Rodriguez-Heredia, Melvin Saccon, Francesco Mosebach, Laura Twachtmann, Manuel Krieger-Liszkay, Anja Duffy, Chris Knell, Robert J Finazzi, Giovanni Hanke, Guy Thomas Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions |
title | Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions |
title_full | Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions |
title_fullStr | Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions |
title_full_unstemmed | Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions |
title_short | Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions |
title_sort | regulation of photosynthetic electron flow on dark to light transition by ferredoxin:nadp(h) oxidoreductase interactions |
topic | Plant Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7984839/ https://www.ncbi.nlm.nih.gov/pubmed/33685582 http://dx.doi.org/10.7554/eLife.56088 |
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