Beatriz Badia, Mariana, Mans, Robert, Lis, Alicia V., Ariel Tronconi, Marcos, Lucia Arias, Cintia, Maurino, Veronica Graciela, Santiago Andreo, Carlos, Fabiana Drincovich, Maria, van Maris, Antonius J. A. and Gerrard Wheeler, Mariel Claudia (2017). Specific Arabidopsis thaliana malic enzyme isoforms can provide anaplerotic pyruvate carboxylation function in Saccharomyces cerevisiae. FEBS J., 284 (4). S. 654 - 666. HOBOKEN: WILEY. ISSN 1742-4658
Full text not available from this repository.Abstract
NAD(P)-malic enzyme (NAD(P)-ME) catalyzes the reversible oxidative decarboxylation of malate to pyruvate, CO2, and NAD(P)H and is present as a multigene family in Arabidopsis thaliana. The carboxylation reaction catalyzed by purified recombinant Arabidopsis NADP-ME proteins is faster than those reported for other animal or plant isoforms. In contrast, no carboxylation activity could be detected in vitro for the NAD-dependent counterparts. In order to further investigate their putative carboxylating role in vivo, Arabidopsis NAD(P)-ME isoforms, as well as the NADP-ME2del2 (with a decreased ability to carboxylate pyruvate) and NADP-ME2R115A (lacking fumarate activation) versions, were functionally expressed in the cytosol of pyruvate carboxylase-negative (Pyc(-)) Saccharomyces cerevisiae strains. The heterologous expression of NADP-ME1, NADP-ME2 (and its mutant proteins), and NADP-ME3 restored the growth of Pyc(-) S. cerevisiae on glucose, and this capacity was dependent on the availability of CO2. On the other hand, NADP-ME4, NAD-ME1, and NAD-ME2 could not rescue the Pyc(-) strains from C-4 auxotrophy. NADP-ME carboxylation activity could be measured in leaf crude extracts of knockout and over-expressing Arabidopsis lines with modified levels of NADP-ME, where this activity was correlated with the amount of NADP-ME2 transcript. These results indicate that specific A. thaliana NADP-ME isoforms are able to play an anaplerotic role in vivo and provide a basis for the study on the carboxylating activity of NADP-ME, which may contribute to the synthesis of C-4 compounds and redox shuttling in plant cells.
| Item Type: | Journal Article | ||||||||||||||||||||||||||||||||||||||||||||
| Creators: |
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| URN: | urn:nbn:de:hbz:38-240716 | ||||||||||||||||||||||||||||||||||||||||||||
| DOI: | 10.1111/febs.14013 | ||||||||||||||||||||||||||||||||||||||||||||
| Journal or Publication Title: | FEBS J. | ||||||||||||||||||||||||||||||||||||||||||||
| Volume: | 284 | ||||||||||||||||||||||||||||||||||||||||||||
| Number: | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Page Range: | S. 654 - 666 | ||||||||||||||||||||||||||||||||||||||||||||
| Date: | 2017 | ||||||||||||||||||||||||||||||||||||||||||||
| Publisher: | WILEY | ||||||||||||||||||||||||||||||||||||||||||||
| Place of Publication: | HOBOKEN | ||||||||||||||||||||||||||||||||||||||||||||
| ISSN: | 1742-4658 | ||||||||||||||||||||||||||||||||||||||||||||
| Language: | English | ||||||||||||||||||||||||||||||||||||||||||||
| Faculty: | Unspecified | ||||||||||||||||||||||||||||||||||||||||||||
| Divisions: | Unspecified | ||||||||||||||||||||||||||||||||||||||||||||
| Subjects: | no entry | ||||||||||||||||||||||||||||||||||||||||||||
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| Refereed: | Yes | ||||||||||||||||||||||||||||||||||||||||||||
| URI: | http://kups.ub.uni-koeln.de/id/eprint/24071 |
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