Mannitol metabolism in brown algae involves a new phosphatase family

Brown algae belong to a phylogenetic lineage distantly related to green plants and animals, and are found predominantly in the intertidal zone, a harsh and frequently changing environment. Because of their unique evolutionary history and of their habitat, brown algae feature several peculiarities in...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 65(2014), 2 vom: 15. Feb., Seite 559-70
1. Verfasser: Groisillier, Agnès (VerfasserIn)
Weitere Verfasser: Shao, Zhanru, Michel, Gurvan, Goulitquer, Sophie, Bonin, Patricia, Krahulec, Stefan, Nidetzky, Bernd, Duan, Delin, Boyen, Catherine, Tonon, Thierry
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Carbon storage Ectocarpus siliculosus HAD (haloacid dehalogenase) superfamily mannitol metabolism. phosphatases primary Algal Proteins mehr... Recombinant Proteins Mannitol 3OWL53L36A Carbon 7440-44-0 Phosphoric Monoester Hydrolases EC 3.1.3.2 mannitol-1-phosphatase EC 3.1.3.22
Beschreibung
Zusammenfassung:Brown algae belong to a phylogenetic lineage distantly related to green plants and animals, and are found predominantly in the intertidal zone, a harsh and frequently changing environment. Because of their unique evolutionary history and of their habitat, brown algae feature several peculiarities in their metabolism. One of these is the mannitol cycle, which plays a central role in their physiology, as mannitol acts as carbon storage, osmoprotectant, and antioxidant. This polyol is derived directly from the photoassimilate fructose-6-phosphate via the action of a mannitol-1-phosphate dehydrogenase and a mannitol-1-phosphatase (M1Pase). Genome analysis of the brown algal model Ectocarpus siliculosus allowed identification of genes potentially involved in the mannitol cycle. Among these, two genes coding for haloacid dehalogenase (HAD)-like enzymes were suggested to correspond to M1Pase activity, and thus were named EsM1Pase1 and EsM1Pase2, respectively. To test this hypothesis, both genes were expressed in Escherichia coli. Recombinant EsM1Pase2 was shown to hydrolyse the phosphate group from mannitol-1-phosphate to produce mannitol but was not active on the hexose monophosphates tested. Gene expression analysis showed that transcription of both E. siliculosus genes was under the influence of the diurnal cycle. Sequence analysis and three-dimensional homology modelling indicated that EsM1Pases, and their orthologues in Prasinophytes, should be seen as founding members of a new family of phosphatase with original substrate specificity within the HAD superfamily of proteins. This is the first report describing the characterization of a gene encoding M1Pase activity in photosynthetic organisms
Beschreibung:Date Completed 25.09.2014
Date Revised 09.01.2024
published: Print-Electronic
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/ert405