Molecular insights into the differences between cyanobacterial and plant LPORs and prolamellar body formation : In vitro studies
Copyright © 2024 The Author(s). Published by Elsevier Masson SAS.. All rights reserved.
| Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 214(2024) vom: 05. Aug., Seite 108935 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
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2024
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| Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
| Schlagworte: | Journal Article Oxidoreductases Acting on CH-CH Group Donors EC 1.3.- protochlorophyllide reductase EC 1.3.1.33 Plant Proteins Bacterial Proteins |
| Zusammenfassung: | Copyright © 2024 The Author(s). Published by Elsevier Masson SAS.. All rights reserved. Light-dependent protochlorophyllide oxidoreductase (LPOR) has captivated the interest of the research community for decades. One reason is the photocatalytic nature of the reaction catalyzed by the enzyme, and the other is the involvement of LPOR in the formation of a paracrystalline lattice called a prolamellar body (PLB) that disintegrates upon illumination, initiating a process of photosynthetic membrane formation. In this paper, we have integrated three traditional methods previously employed to study the properties of the enzyme: molecular biology, spectroscopy, and electron microscopy. We found that for cyanobacterial LPOR, substrates binding appears to be independent of lipids, with membrane interaction primarily affecting the enzyme post-reaction, with MGDG and PG having opposite effects on SynPOR. In contrast, plant isoforms exhibit sequence alterations, rendering the enzyme effective in substrate binding mainly in the presence of anionic lipids, depending on residues at positions 122, 312, and 318. Moreover, we demonstrated that the interaction with MGDG could initially serve as enhancement of the substrate specificity towards monovinyl-protochlorophyllide (Pchlide). We have shown that the second LPOR isoforms of eudicots and monocots accumulated mutations that made these variants less and more dependent on anionic lipids, respectively. Finally, we have shown that in the presence of Pchlide, NADP+, and the lipids, plant but not cyanobacterial LPOR homolog remodel membranes into the cubic phase. The cubic phase is preserved if samples supplemented with NADP + are enriched with NADPH. The results are discussed in the evolutionary context, and the model of PLB formation is presented |
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| Beschreibung: | Date Completed 04.08.2024 Date Revised 04.08.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2690 |
| DOI: | 10.1016/j.plaphy.2024.108935 |