Photosystem-II D1 protein mutants of Chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of H-bond network at QB site

Abstract Photosystem II (PSII) reaction centre D1 protein of oxygenic phototrophs is pivotal for sustaining photosynthesis. Also, it is targeted by herbicides and herbicide-resistant weeds harbour single amino acid substitutions in D1. Conservation of D1 primary structure is seminal in the photosynt...

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Autores principales: Amina Antonacci, Maya D. Lambreva, Andrea Margonelli, Anatoly P. Sobolev, Sandro Pastorelli, Ivo Bertalan, Udo Johanningmeier, Vladimir Sobolev, Ilan Samish, Marvin Edelman, Vesa Havurinne, Esa Tyystjärvi, Maria T. Giardi, Autar K. Mattoo, Giuseppina Rea
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Publicado: Nature Portfolio 2018
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spelling oai:doaj.org-article:d7d59f7fe000484b90acc5aa2ca7929f2021-12-02T11:40:46ZPhotosystem-II D1 protein mutants of Chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of H-bond network at QB site10.1038/s41598-018-33146-y2045-2322https://doaj.org/article/d7d59f7fe000484b90acc5aa2ca7929f2018-10-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-33146-yhttps://doaj.org/toc/2045-2322Abstract Photosystem II (PSII) reaction centre D1 protein of oxygenic phototrophs is pivotal for sustaining photosynthesis. Also, it is targeted by herbicides and herbicide-resistant weeds harbour single amino acid substitutions in D1. Conservation of D1 primary structure is seminal in the photosynthetic performance in many diverse species. In this study, we analysed built-in and environmentally-induced (high temperature and high photon fluency – HT/HL) phenotypes of two D1 mutants of Chlamydomonas reinhardtii with Ala250Arg (A250R) and Ser264Lys (S264K) substitutions. Both mutations differentially affected efficiency of electron transport and oxygen production. In addition, targeted metabolomics revealed that the mutants undergo specific differences in primary and secondary metabolism, namely, amino acids, organic acids, pigments, NAD, xanthophylls and carotenes. Levels of lutein, β-carotene and zeaxanthin were in sync with their corresponding gene transcripts in response to HT/HL stress treatment in the parental (IL) and A250R strains. D1 structure analysis indicated that, among other effects, remodelling of H-bond network at the QB site might underpin the observed phenotypes. Thus, the D1 protein, in addition to being pivotal for efficient photosynthesis, may have a moonlighting role in rewiring of specific metabolic pathways, possibly involving retrograde signalling.Amina AntonacciMaya D. LambrevaAndrea MargonelliAnatoly P. SobolevSandro PastorelliIvo BertalanUdo JohanningmeierVladimir SobolevIlan SamishMarvin EdelmanVesa HavurinneEsa TyystjärviMaria T. GiardiAutar K. MattooGiuseppina ReaNature PortfolioarticlePhotosystem II (PSII)Metabolic RewiringZeaxanthinHigh Photon FluencePhotosynthetic PerformanceMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-14 (2018)
institution DOAJ
collection DOAJ
language EN
topic Photosystem II (PSII)
Metabolic Rewiring
Zeaxanthin
High Photon Fluence
Photosynthetic Performance
Medicine
R
Science
Q
spellingShingle Photosystem II (PSII)
Metabolic Rewiring
Zeaxanthin
High Photon Fluence
Photosynthetic Performance
Medicine
R
Science
Q
Amina Antonacci
Maya D. Lambreva
Andrea Margonelli
Anatoly P. Sobolev
Sandro Pastorelli
Ivo Bertalan
Udo Johanningmeier
Vladimir Sobolev
Ilan Samish
Marvin Edelman
Vesa Havurinne
Esa Tyystjärvi
Maria T. Giardi
Autar K. Mattoo
Giuseppina Rea
Photosystem-II D1 protein mutants of Chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of H-bond network at QB site
description Abstract Photosystem II (PSII) reaction centre D1 protein of oxygenic phototrophs is pivotal for sustaining photosynthesis. Also, it is targeted by herbicides and herbicide-resistant weeds harbour single amino acid substitutions in D1. Conservation of D1 primary structure is seminal in the photosynthetic performance in many diverse species. In this study, we analysed built-in and environmentally-induced (high temperature and high photon fluency – HT/HL) phenotypes of two D1 mutants of Chlamydomonas reinhardtii with Ala250Arg (A250R) and Ser264Lys (S264K) substitutions. Both mutations differentially affected efficiency of electron transport and oxygen production. In addition, targeted metabolomics revealed that the mutants undergo specific differences in primary and secondary metabolism, namely, amino acids, organic acids, pigments, NAD, xanthophylls and carotenes. Levels of lutein, β-carotene and zeaxanthin were in sync with their corresponding gene transcripts in response to HT/HL stress treatment in the parental (IL) and A250R strains. D1 structure analysis indicated that, among other effects, remodelling of H-bond network at the QB site might underpin the observed phenotypes. Thus, the D1 protein, in addition to being pivotal for efficient photosynthesis, may have a moonlighting role in rewiring of specific metabolic pathways, possibly involving retrograde signalling.
format article
author Amina Antonacci
Maya D. Lambreva
Andrea Margonelli
Anatoly P. Sobolev
Sandro Pastorelli
Ivo Bertalan
Udo Johanningmeier
Vladimir Sobolev
Ilan Samish
Marvin Edelman
Vesa Havurinne
Esa Tyystjärvi
Maria T. Giardi
Autar K. Mattoo
Giuseppina Rea
author_facet Amina Antonacci
Maya D. Lambreva
Andrea Margonelli
Anatoly P. Sobolev
Sandro Pastorelli
Ivo Bertalan
Udo Johanningmeier
Vladimir Sobolev
Ilan Samish
Marvin Edelman
Vesa Havurinne
Esa Tyystjärvi
Maria T. Giardi
Autar K. Mattoo
Giuseppina Rea
author_sort Amina Antonacci
title Photosystem-II D1 protein mutants of Chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of H-bond network at QB site
title_short Photosystem-II D1 protein mutants of Chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of H-bond network at QB site
title_full Photosystem-II D1 protein mutants of Chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of H-bond network at QB site
title_fullStr Photosystem-II D1 protein mutants of Chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of H-bond network at QB site
title_full_unstemmed Photosystem-II D1 protein mutants of Chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of H-bond network at QB site
title_sort photosystem-ii d1 protein mutants of chlamydomonas reinhardtii in relation to metabolic rewiring and remodelling of h-bond network at qb site
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/d7d59f7fe000484b90acc5aa2ca7929f
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