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

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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 C hlamydomonas 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 Q _B 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.

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Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses.

Michihiro Suga, Fusamichi Akita, Kunio Hirata … (2015)

Photosynthesis converts light energy into biologically useful chemical energy vital to life on Earth. The initial reaction of photosynthesis takes place in photosystem II (PSII), a 700-kilodalton homodimeric membrane protein complex that catalyses photo-oxidation of water into dioxygen through an S-state cycle of the oxygen evolving complex (OEC). The structure of PSII has been solved by X-ray diffraction (XRD) at 1.9 ångström resolution, which revealed that the OEC is a Mn4CaO5-cluster coordinated by a well defined protein environment. However, extended X-ray absorption fine structure (EXAFS) studies showed that the manganese cations in the OEC are easily reduced by X-ray irradiation, and slight differences were found in the Mn-Mn distances determined by XRD, EXAFS and theoretical studies. Here we report a 'radiation-damage-free' structure of PSII from Thermosynechococcus vulcanus in the S1 state at a resolution of 1.95 ångströms using femtosecond X-ray pulses of the SPring-8 ångström compact free-electron laser (SACLA) and hundreds of large, highly isomorphous PSII crystals. Compared with the structure from XRD, the OEC in the X-ray free electron laser structure has Mn-Mn distances that are shorter by 0.1-0.2 ångströms. The valences of each manganese atom were tentatively assigned as Mn1D(III), Mn2C(IV), Mn3B(IV) and Mn4A(III), based on the average Mn-ligand distances and analysis of the Jahn-Teller axis on Mn(III). One of the oxo-bridged oxygens, O5, has significantly longer distances to Mn than do the other oxo-oxygen atoms, suggesting that O5 is a hydroxide ion instead of a normal oxygen dianion and therefore may serve as one of the substrate oxygen atoms. These findings provide a structural basis for the mechanism of oxygen evolution, and we expect that this structure will provide a blueprint for the design of artificial catalysts for water oxidation.

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Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II.

Bernhard Loll, Jan Kern, Wolfram Saenger … (2005)

Oxygenic photosynthesis in plants, algae and cyanobacteria is initiated at photosystem II, a homodimeric multisubunit protein-cofactor complex embedded in the thylakoid membrane. Photosystem II captures sunlight and powers the unique photo-induced oxidation of water to atmospheric oxygen. Crystallographic investigations of cyanobacterial photosystem II have provided several medium-resolution structures (3.8 to 3.2 A) that explain the general arrangement of the protein matrix and cofactors, but do not give a full picture of the complex. Here we describe the most complete cyanobacterial photosystem II structure obtained so far, showing locations of and interactions between 20 protein subunits and 77 cofactors per monomer. Assignment of 11 beta-carotenes yields insights into electron and energy transfer and photo-protection mechanisms in the reaction centre and antenna subunits. The high number of 14 integrally bound lipids reflects the structural and functional importance of these molecules for flexibility within and assembly of photosystem II. A lipophilic pathway is proposed for the diffusion of secondary plastoquinone that transfers redox equivalents from photosystem II to the photosynthetic chain. The structure provides information about the Mn4Ca cluster, where oxidation of water takes place. Our study uncovers near-atomic details necessary to understand the processes that convert light to chemical energy.

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Learning the Languages of the Chloroplast: Retrograde Signaling and Beyond.

Kai Chan, Su Phua, Peter A. Crisp … (2016)

The chloroplast can act as an environmental sensor, communicating with the cell during biogenesis and operation to change the expression of thousands of proteins. This process, termed retrograde signaling, regulates expression in response to developmental cues and stresses that affect photosynthesis and yield. Recent advances have identified many signals and pathways-including carotenoid derivatives, isoprenes, phosphoadenosines, tetrapyrroles, and heme, together with reactive oxygen species and proteins-that build a communication network to regulate gene expression, RNA turnover, and splicing. However, retrograde signaling pathways have been viewed largely as a means of bilateral communication between organelles and nuclei, ignoring their potential to interact with hormone signaling and the cell as a whole to regulate plant form and function. Here, we discuss new findings on the processes by which organelle communication is initiated, transmitted, and perceived, not only to regulate chloroplastic processes but also to intersect with cellular signaling and alter physiological responses.

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Author and article information

Contributors

Autar K. Mattoo:

ORCID: http://orcid.org/0000-0001-9226-7164

Autar.Mattoo@ars.usda.gov

Giuseppina Rea:

ORCID: http://orcid.org/0000-0001-7353-727X

giuseppina.rea@ic.cnr.it

Journal

Journal ID (nlm-ta): Sci Rep

Journal ID (iso-abbrev): Sci Rep

Title: Scientific Reports

Publisher: Nature Publishing Group UK (London )

ISSN (Electronic): 2045-2322

Publication date (Electronic): 3 October 2018

Publication date PMC-release: 3 October 2018

Publication date Collection: 2018

Volume: 8

Electronic Location Identifier: 14745

Affiliations

[1 ]ISNI 0000 0001 1940 4177, GRID grid.5326.2, Institute of Crystallography, , National Research Council of Italy, ; Via Salaria Km 29,3 00015, Monterotondo Stazione, Rome Italy

[2 ]ISNI 0000 0001 1940 4177, GRID grid.5326.2, Institute of Chemical Methodologies, , National Research Council of Italy, ; Via Salaria km 29,3 00015, Monterotondo Stazione, Rome Italy

[3 ]Present Address: Neotron S.p.a., Santa Maria di Mugnano, Modena, Italy

[4 ]Martin-Luther-University, Plant Physiology Institute, Weinbergweg 10, D-06120 Halle Saale, Germany

[5 ]ISNI 0000 0004 0604 7563, GRID grid.13992.30, Department of Plant and Environmental Sciences, , Weizmann Institute of Science, ; Rehovot, Israel

[6 ]Present Address: Amai Proteins Ltd., 2 Bergman St., Rehovot, Israel

[7 ]ISNI 0000 0001 2097 1371, GRID grid.1374.1, Department of Biochemistry/Molecular Plant Biology, , FI-20014, University of Turku, ; Turku, Finland

[8 ]ISNI 0000 0004 0404 0958, GRID grid.463419.d, The Henry A Wallace Beltsville Agricultural Research Centre, United States Department of Agriculture, , Sustainable Agricultural Systems Laboratory, ; Beltsville, Maryland 20705 USA

Author information

Maya D. Lambreva http://orcid.org/0000-0001-5750-0899

Autar K. Mattoo http://orcid.org/0000-0001-9226-7164

Giuseppina Rea http://orcid.org/0000-0001-7353-727X

Article

Publisher ID: 33146

DOI: 10.1038/s41598-018-33146-y

PMC ID: 6170454

PubMed ID: 30283151

SO-VID: 4b1e1c26-a24e-4ec0-97ff-f9721d78c9bc

License:

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

History

Date received : 29 March 2018

Date accepted : 21 September 2018

Funding

Funded by: FundRef https://doi.org/10.13039/501100004963, EC | Seventh Framework Programme (European Union Seventh Framework Programme);

Award ID: FP7-SDME-232522

Award Recipient : Maya D. Lambreva

Funded by: FundRef https://doi.org/10.13039/100007917, USDA | Agricultural Research Service (ARS);

Award ID: 8042-21000-142-00D

Award Recipient : Autar K. Mattoo

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

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Most cited references 53

Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses.

Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II.

Learning the Languages of the Chloroplast: Retrograde Signaling and Beyond.

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