The ALDH21 gene found in lower plants and some vascular plants codes for a NADP(+) -dependent succinic semialdehyde dehydrogenase
| Autor: | Radka Končitíková, Armelle Vigouroux, David Kopečný, Lenka Jašková, Jan Vilím, Martina Kopečná, Klaus von Schwartzenberg, Eva Hajkova, Solange Moréra, Pierre Briozzo, Marek Šebela |
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| Přispěvatelé: | Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Microbiologie et enzymologie structurale (MESB3S), Département Biochimie, Biophysique et Biologie Structurale (B3S), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Arginine [SDV]Life Sciences [q-bio] Aldehyde dehydrogenase Plant Science Mitochondrion Physcomitrella patens Cofactor structure-function Succinic semialdehyde 03 medical and health sciences chemistry.chemical_compound GABA aldehyde dehydrogenase Oxidoreductase Genetics succinic semialdehyde ALDH5 x-ray crystallography chemistry.chemical_classification biology ALDH21 Cell Biology 15. Life on land biology.organism_classification 030104 developmental biology chemistry Biochemistry biology.protein NAD+ kinase site-directed mutagenesis |
| Zdroj: | The Plant Journal: For Cell and Molecular Biology The Plant Journal: For Cell and Molecular Biology, 2017, 92 (2), pp.229-243. ⟨10.1111/tpj.13648⟩ |
| Popis: | Lower plant species including some green algae, non-vascular plants (bryophytes) as well as the oldest vascular plants (lycopods) and ferns (monilophytes) possess a unique aldehyde dehydrogenase (ALDH) gene named ALDH21, which is upregulated during dehydration. However, the gene is absent in flowering plants. Here, we show that ALDH21 from the moss Physcomitrella patens codes for a tetrameric NADP(+) -dependent succinic semialdehyde dehydrogenase (SSALDH), which converts succinic semialdehyde, an intermediate of the γ-aminobutyrate (GABA) shunt pathway, into succinate in the cytosol. NAD(+) is a very poor coenzyme for ALDH21 unlike for mitochondrial SSALDHs (ALDH5), which are the closest related ALDH members. Structural comparison between the apoform and the coenzyme complex reveal that NADP(+) binding induces a conformational change of the loop carrying Arg-228, which seals the NADP(+) in the coenzyme cavity via its 2'-phosphate and α-phosphate groups. The crystal structure with the bound product succinate shows that its carboxylate group establishes salt bridges with both Arg-121 and Arg-457 and a hydrogen bond with Tyr-296. While both arginine residues are pre-formed for substrate/product binding, Tyr-296 moves by more than 1 Å. Both R121A and R457A variants are almost inactive demonstrating a key role of each arginine in catalysis. Our study implies that bryophytes but presumably also some green algae, lycopods and ferns, which carry both ALDH21 and ALDH5 genes, can oxidize SSAL to succinate in both cytosol and mitochondria indicating more diverse GABA shunt pathway compared with higher plants carrying only the mitochondrial ALDH5. This article is protected by copyright. All rights reserved. |
| Databáze: | OpenAIRE |
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