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Characterization of a nonphotochemical quenching-deficient Arabidopsis mutant possessing an intact PsbS protein, xanthophyll cycle and lumen acidification
Abstract
Arabidopsis thaliana plants grown from ethyl methane sulfonate-treated seeds were screened for so-called que mutants, which are affected in non-photochemical energy quenching. Based on video imaging of chlorophyll fluorescence an energy dissipation mutant, que1, was identified, isolated and characterized. Similar to the npq mutants, the que1 mutant showed a drastically reduced capacity for pH-dependent energy dissipation, qE, but without affecting the Delta pH-dependent conformational changes at 535 nm (DeltaA (535)), which have been supposed to be obligatorily correlated with qE and to reflect pH-regulated binding of zeaxanthin to the PsbS protein. Western blot and DNA sequence analysis revealed that neither a reduced expression of the PsbS protein nor a mutation in the PsbS gene was responsible for the missing qE in que1. Measurements of 9-aminoacridine fluorescence quenching showed that the acidification of the thylakoid lumen was also not affected in the mutant. Furthermore, que1 was able to convert violaxanthin to zeaxanthin. However, unusual characteristics of zeaxanthin formation in the mutant pointed at an altered availability of violaxanthin for de-epoxidation. This was further accompanied by a decrease of the photochemical quenching of chlorophyll fluorescence (qP), an increase of the portion of oxidized P700 and a reduction of the electron transport rate. These characteristics indicate changes in the organization of the thylakoid membrane that affect linear electron transport (but not lumen acidification) and the formation of energy dissipation in photosystem II. Preliminary genetic analysis revealed that the phenotype of que1 is related to two different mutations, mapped to the lower arms of chromosomes 1 and 4.
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“These predictions are broadly in line with experimental measurements for Arabidopsis (Kalituho et al., 2006; Khanal et al., 2017).”
From Leaf Energy Balance Requires Mitochondrial Respiration and Export of Chloroplast NADPH in the Light (2019) · cites this paper as Kalituho et al., 2006
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Research works printed but not linked: 1
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Metadata
- Authors
- Kalituho, L., Graßes, T., Graf, M., Rech, J., & Jahns, P.
- Affiliations
- Heinrich Heine University Düsseldorf (DE)
- Corresponding author
- Jahns, Peter
- ORCID
- Jahns, Peter
- Venue
- Planta
- Published
- 2005-09-01
- Volume
- 223
- Issue
- 3
- Pages
- 532-541
- ISSN
- 0032-0935 (ISSN-L)
- 1432-2048
- OpenAlex
- W2020616951
- Cited by
- 17
- References
- 62
- Citations by year
- 2022: 1 · 2019: 2 · 2018: 1 · 2017: 1 · 2013: 1 · 2012: 1
- FWCI
- 0.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Planta (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Keywords
- non-photochemical quenching, PsbS protein, xanthophyll cycle, violaxanthin de-epoxidation, photochemical quenching, P700 oxidation, linear electron transport, photosystem II, thylakoid membrane organization, Arabidopsis thaliana, EMS mutagenesis
- MeSH terms
- Absorption, Chlorophyll, Chromosome Mapping, Electron Transport, Fluorescence, Hydrogen-Ion Concentration, Light, Mutation, Photosynthesis, Arabidopsis, Sequence Analysis, DNA, Plant Leaves, Thylakoids, Xanthophylls, Arabidopsis Proteins, Photosynthetic Reaction Center Complex Proteins, Photosystem II Protein Complex, Light-Harvesting Protein Complexes, Zeaxanthins
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