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 Q 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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http://dx.doi.org/10.1038/s41598-018-33146-y | DOI Listing |
J Photochem Photobiol B
December 2024
Department of Biology, University of New Brunswick, Fredericton E3B5A3, NB, Canada. Electronic address:
Under ideal conditions, Chlamydomonas reinhardtii can photoacclimate to excess light through various short- and long-term mechanisms. However, how microalgae handle excess light stress once they exit exponential growth, and especially in stationary phase, is less understood. Our study explored C.
View Article and Find Full Text PDFPhysiol Plant
December 2024
Institute of Crystallography, National Research Council, Monterotondo Stazione (RM), Italy.
An in silico redesign of the secondary quinone electron acceptor (Q) binding pocket of the D1 protein of Photosystem II (PSII) suggested that mutations of the F265 residue would affect atrazine binding. Chlamydomonas reinhardtii mutants F265T and F265S were produced to obtain atrazine-hypersensitive strains for biosensor applications, and the mutants were indeed found to be more atrazine-sensitive than the reference strain IL. Fluorescence and thermoluminescence data agree with a weak driving force and confirm slow electron transfer but cannot exclude an additional effect on protonation of the secondary quinone.
View Article and Find Full Text PDFSci Rep
December 2024
Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, 70803, USA.
This study investigates the control of ciliary beat patterns during ammonium chemotaxis in the model ciliate microalga Chlamydomonas reinhardtii. Screening the chemotaxis response of mutant strains with ciliary defects revealed that a strain lacking CAV2, the alpha subunit of the voltage-gated calcium channel, is deficient in ammonium chemotaxis. CAV2 regulates the switching of the ciliary beat pattern from the asymmetric to the symmetric waveform.
View Article and Find Full Text PDFJ Environ Sci (China)
June 2025
College of Resources and Environmental Sciences, Nanjing Agricultural University, Nanjing 210095, China. Electronic address:
Arsenic (As) pollution seriously threatens human and ecological health. Microalgal cell wall and extracellular polymeric substances (EPS) are known to interact with As, but their roles in the As resistance, accumulation and speciation in microalgae remain unclear. Here, we used two strains of Chlamydomonas reinhardtii, namely CC-125 (wild type) and CC-503 (cell wall-deficient mutant), to examine the algal growth, EPS synthesis, As adsorption, absorption and transformation under 10-1000 µg/L As(III) and As(V) treatments for 96 h.
View Article and Find Full Text PDFmSphere
December 2024
Department of Biological Sciences, Graduate School of Science, Osaka University, Osaka, Japan.
Unlabelled: Motile flagella (also called "motile cilia") play a variety of important roles in lower and higher eukaryotes, including cellular motility and fertility. Flagellar motility is driven by several species of the gigantic motor-protein complexes, flagellar dyneins, that reside within these organelles. Among the flagellar-dynein species, a hetero-dimeric dynein called "IDA f/I1" has been shown to be particularly important in controlling the flagellar waveform, and defects in this dynein species in humans cause ciliopathies such as multiple morphological abnormalities of the flagella and asthenoteratozoospermia.
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